Method For Preparing Maltogenic Alpha-Amylase Variants

ABSTRACT

The inventors have modified the amino acid sequence of a maltogenic alpha-amylase to obtain variants with improved properties, based on the three-dimensional structure of the maltogenic alpha-amylase Novamyl. The variants have altered physicochemical properties., e.g. an altered pH optimum, improved thermostability, increased specific activity, an altered cleavage pattern or an increased ability to reduce retrogradation of starch or staling of bread.

CROSS-REFERENCE TO RELATED APPLICATIONS

This application is a continuation of U.S. application Ser. No.13/010,219 filed on Jan. 20, 2011 (pending), which is a continuation ofU.S. application Ser. No. 12/413,758 filed on Mar. 30, 2009 (now U.S.Pat. No. 7,908,094), which is a continuation of U.S. application Ser.No. 11/037,573 (abandoned) filed on Jan. 18, 2005, which is acontinuation of U.S. application Ser. No. 09/607,142 (now U.S. Pat. No.6,876,932) filed Jun. 29, 2000, which is a divisional of U.S.application Ser. No. 09/386,607 (now U.S. Pat. No. 6,162,628), filedAug. 31, 1999, which is a continuation in part of PCT/DK99/00088, filedFeb. 26, 1999 which claims priority or the benefit under 35 U.S.C. 119of Danish application no. 98/00269, filed Feb. 27, 1998 and U.S.Provisional application No. 60/077,795, filed Mar. 12, 1998, thecontents of which are fully incorporated herein by reference.

FIELD OF THE INVENTION

The present invention relates to variants of maltogenic amylase and tomethods of constructing such variants.

BACKGROUND OF THE INVENTION

Maltogenic alpha-amylase (glucan 1,4-α-maltohydrolase, E.C. 3.2.1.133)is able to hydrolyze amylose and amylopectin to maltose in thealpha-configuration, and is also able to hydrolyze maltotriose as wellas cyclodextrin.

A maltogenic alpha-amylase from Bacillus (EP 120 693) is commerciallyavailable under the trade name Novamyl® (product of Novo Nordisk A/S,Denmark) and is widely used in the baking industry as an anti-stalingagent due to its ability to reduce retrogradation of starch (WO91/04669). It is most active at 60-70° C. (Christophersen, C., et al.,1997, Starch, vol. 50, No. 1, 39-45).

Novamyl® shares several characteristics with cyclodextringlucanotransferases (CGTases), including sequence homology (HenrissatB., Bairoch A. 1996) and formation of transglycosylation products(Christophersen, C., et al., 1997, Starch, vol. 50, No. 1, 39-45).Cyclomaltodextrin glucanotransferase (E.C. 2.4.1.19), also designatedcyclodextrin glucanotransferase or cyclodextrin glycosyltransferase,abbreviated herein as CGTase, catalyses the conversion of starch andsimilar substrates into cyclomaltodextrins via an intramoleculartransglycosylation reaction, thereby forming cyclomaltodextrins (or CD)of various sizes.

CGTases are widely distributed and from several different bacterialsources, including Bacillus, Brevibacterium, Clostridium,Corynebacterium, Klebsiella, Micrococcus, Thermoanaerobacter andThermoanaerobacterium have been extensively described in the literature.A CGTase produced by Thermoanaerobacter sp. has been reported in NormanB E, Jørgensen S T; Denpun Kaqaku 1992 39 99-106, and WO 89/03421, andthe amino acid sequence has been disclosed in WO 96/33267. The sequenceof CGTases from Thermoanaerobacterium thermosulfurigenes and fromBacillus circulansis available on the Internet (SCOP or PDF home pages)as pdf file 1CIU, and the sequence of a CGTase from B. circulans isavailable as pdf file 1CDG.

Tachibana, Y., Journal of Fermentation and Bioengineering, 83 (6),540-548 (1997) describes the cloning and expression of a CGTase.Variants of CGTases have been described by Kim, Y. H., Biochemistry andMolecular Biology International, 41 (2), 227-234 (1997); Sin K-A,Journal of Biotechnology, 32 (3), 283-288 (1994); D Penning a,Biochemistry, 34 (10), 3368-3376 (1995); and WO 96/33267.

Recently, the tertiary structure of several CGTases have been reported.Hofman et al. [Hofman B E, Bender H, Schultz G E; J. Mol. Biol. 1989 209793-800] and Klein & Schulz [Klein C, Schulz G E; J. Mol. Biol. 1991 217737-750] report the tertiary structure of a CGTase derived from Bacilluscirculans Strain 8, Kubota et al. [Kubota M, Matsuura Y, Sakai S andKatsube Y; Denpun Kagaku 1991 38 141-146] report the tertiary structureof a CGTase derived from Bacillus stearothermophilus TC-91, Lawson etal. [Lawson C L, van Montfort R, Strokopytov B, Rozeboom H J, Kalk K H,de Vries G E, Penning a D, Dijkhuizen L, and Dijkstra B W; J. Mol. Biol.1994 236 590-600] report the tertiary structure of a CGTase derived fromBacillus circulans Strain 251, Strokopytov et al. [Strokopytov B,Penning a D, Rozeboom H J; Kalk K H, Dijkhuizen L and Dijkstra B W;Biochemistry 1995 34 2234-2240] report the tertiary structure of aCGTase derived from Bacillus circulans Strain 251, which CGTase has beencomplexed with acarbose, an effective CGTase inhibitor, and Knegtel etal. [Knegtel R M A, Wind R D, Rozeboom H J, Kalk K H, Buitelaar R M,Dijkhuizen L and Dijkstra B W; J. Mol. Biol. 1996 256 611-622] reportthe tertiary structure of a CGTase derived from Thermoanaerobacteriumthermosulfurigenes.

BRIEF DESCRIPTION OF THE FIGURE

FIG. 1 shows the plasmid pLBei010, which contains the Bacillusstearothermophilus maltogenic amylase gene.

DETAILED DISCLOSURE OF THE INVENTION

The inventors have found that the anti-staling effect of a maltogenicamylase can be improved by using a variant having increasedthermostability. Further, they found that such a variant improves thesoftness of baked products in the initial period after baking,particularly the first 24 hours after baking, so that the baked producthas improved softness, both when eaten on the same day and when storedfor several days after baking.

Accordingly, the invention provides a polypeptide which:

a) has maltogenic amylase activity;

b) has at least 70% identity to SEQ ID NO: 2,

c) has optimum maltogenic amylase activity in the range pH 3.5-7.0(preferably 4-5.5), and

d) shows a residual maltogenic amylase activity of at least 25% afterincubation with 1 mM Ca⁺⁺ at pH 4.3, 80° C. for 15 minutes.

The inventors found that thermostable variants can be prepared by randomDNA mutagenesis followed by screening for thermostable variants. Thus,the invention also provides a method of preparing a maltogenic amylasevariant having improved anti-staling properties, which method comprises

a) subjecting a DNA sequence encoding the maltogenic amylase to randommutagenesis,

b) expressing the mutated DNA sequence obtained in step (a) in a hostcell, and

c) screening for host cells expressing a mutated maltogenic amylasewhich shows a higher thermostability, and

d) preparing the mutated maltogenic amylase expressed by the host cells.

Further, the inventors have modified the amino acid sequence of amaltogenic alpha-amylase to obtain variants with improved properties,based on the three-dimensional structure of the maltogenic alpha-amylaseNovamyl. The variants have altered physicochemical properties., e.g. analtered pH optimum, improved thermostability, increased specificactivity, an altered cleavage pattern or an increased ability to reduceretrogradation of starch or staling of bread.

Accordingly, the present invention provides a method of constructing avariant of a parent maltogenic alpha-amylase, wherein the variant has atleast one altered property as compared to said parent maltogenicalpha-amylase, which method comprises:

i) analyzing the structure of the maltogenic alpha-amylase to identify,on the basis of an evaluation of structural considerations, at least oneamino acid residue or at least one structural region of the maltogenicalpha-amylase, which is of relevance for altering said property;

ii) constructing a variant of the maltogenic alpha-amylase, which ascompared to the parent, has been modified in the amino acid residue orstructural part identified in i) so as to alter said property; and

iii) testing the resulting maltogenic alpha-amylase variant for saidproperty.

The property which may be altered by the above methods of the presentinvention may be, e.g., stability, pH dependent activity, ability toreduce retrogradation of starch or staling of bread, specific activity,or substrate specificity. Thus, the variant may have, e.g., increasedthermostability or higher activity at a lower pH an altered pH optimum,improved thermostability, increased specific activity or increasedability to reduce retrogradation of starch or staling of bread

In still further aspects the invention relates to variants of amaltogenic alpha-amylase, the DNA encoding such variants and methods ofpreparing the variants. Finally, the invention relates to the use of thevariants for various industrial purposes, in particular baking.

Maltogenic Alpha-Amylase

The maltogenic alpha-amylase is an enzyme classified in EC 3.2.1.133.The enzymatic activity does not require a non-reducing end on thesubstrate and the primary enzymatic activity results in the degradationof amylopectin and amylose to maltose and longer maltodextrins. It isable to hydrolyze amylose and amylopectin to maltose in thealpha-configuration, and is also able to hydrolyze maltotriose as wellas cyclodextrin.

A particularly preferred maltogenic alpha-amylase is the amylase clonedfrom Bacillus as described in EP 120 693 (hereinafter referred to asNovamyl). Novamyl has the amino acid sequence set forth in amino acids1-686 of SEQ ID NO: 2. Novamyl is encoded in the gene harbored in theBacillus strain NCIB 11837 which has the nucleic acid sequence set forthin SEQ ID NO:1. The three-dimensional structure of Novamyl is describedbelow.

In general, a preferred maltogenic alpha-amylase should have one or moreof the following properties:

i) a three dimensional structural homology to Novamyl,

ii) an amino acid sequence having at least 70% identity to SEQ ID NO: 2,preferably at least 80% or 90%, e.g. 95% or 98%,

iii) a DNA sequence which hybridizes to the DNA sequence set forth inSEQ ID NO:1 or to the DNA sequence encoding Novamyl harbored in theBacillus strain NCIB 11837;

iv) a calcium binding site comprising a coordination equivalent to abackbone carbonyl atom from Asn77, sidechain atom OE2 and OE1 fromGlu102, a sidechain atom OD1 from Asp79, a sidechain atom OD1 fromAsp76, and a sidechain atom OE1 from Glu101, and one water molecule WATV21, atom OW0, wherein the positions are as shown in Appendix 1;

v) a sequence of five amino acids corresponding to Pro-Ala-Gly-Phe-Serin a position equivalent to residues 191-195 in the amino acid sequenceshown in SEQ ID NO: 2; and

The structural homology referred to above in i) is based on othersequence homologies, hydrophobic cluster analysis or by reversethreading (Huber, T; Torda, AE, PROTEIN SCIENCE Vol. 7, No. 1 pp.142-149 (1998)) and which by any of these methods is predicted to havethe same tertiary structure as Novamyl, wherein the tertiary structurerefers to the overall folding or the folding of Domains A, B, and C,more preferably including Domain D, and most preferably including DomainE. Alternatively, a structural alignment between Novamyl and amaltogenic alpha-amylase may be used to identify equivalent positions.

The calcium binding site referred to above in iv) is based on a calciumbinding site identified in the three-dimensional structure of Novamyl,and is discussed below in the section “Calcium binding sites.”

The “equivalent position” referred to above in v) is based on amino acidor DNA sequence alignment or structural homology using methods known inthe art.

Three-Dimensional Structure of Maltogenic Alpha-Amylase

Novamyl was used to elucidate the three-dimensional structure formingthe basis for the present invention.

The structure of Novamyl was solved in accordance with the principle forx-ray crystallographic methods, for example, as given in X-Ray StructureDetermination, Stout, G. K. and Jensen, L. H., John Wiley & Sons, Inc.NY, 1989.

The structural coordinates for the solved crystal structure of Novamylat 2.2 Å resolution using the isomorphous replacement method are givenin standard PDB format (Protein Data Bank, Brookhaven NationalLaboratory, Brookhaven, Conn.) as set forth in Appendix 1. It is to beunderstood that Appendix 1 forms part of the present application. In thecontext of Appendix 1, the following abbreviations are used: CA refersto calcium ion or alpha-carbon atom of the polypeptide backbone, WATrefers to water or to calcium, MAL refers to maltose, HEX refers to acarbohydrate unit of a substrate analogue, and SUL refers to a sulfateion.

Amino acid residues of the enzyme are identified herein by theirrespective one- or three-letter amino acid code.

The structure of said maltogenic alpha-amylase is made up of fiveglobular domains, ordered A, B, C, D and E. The domains can be definedas being residues 1-132 and 204-403 for Domain A, residues 133-203 forDomain B, residues 404-496 for Domain C, residues 497-579 for Domain D,and residues 580-686 for Domain E, wherein the numbering refers to theamino acid sequence in SEQ ID NO: 2. Features of Domains A, B, and C ofparticular interest are described below.

Domain A

Domain A is the largest domain and contains the active site whichcomprises a cluster of three amino acid residues, D329, D228 and E256,spatially arranged at the bottom of a cleft in the surface of theenzyme. The structure of Domain A shows an overall fold in common withthe α-amylases for which the structure is known, viz. the (beta/alpha) 8barrel with eight central beta strands (numbered 1-8) and eight flankinga-helices. The β-barrel is defined by McGregor op. cit. The C-terminalend of the beta strand 1 is connected to helix 1 by a loop denoted loop1 and an identical pattern is found for the other loops, although theloops show some variation in size and some can be quite extensive.

The eight central beta-strands in the (beta/alpha) 8 barrel superimposereasonably well with the known structures of CGTases. This part of thestructure, including the close surroundings of the active site locatedat the C-terminal end of the beta-strands, shows a high degree ofidentity with CGTases.

In contrast, the loops connecting the beta-strands and alpha helicesdisplay a high degree of variation from the known structures of CGTases.These loops constitute the structural context of the active site, andthe majority of the contacts to the substrate is found among residueslocated in these loops. Distinguishing characteristics such as substratespecificity, substrate binding, pH activity profile, substrate cleavagepattern, and the like, are determined by specific amino acids and thepositions they occupy in these loops. In Novamyl Domain A contains twocalcium binding sites, one of which is homologous to the calcium bindingsite in CGTases; the other is unique to Novamyl.

The structure of the calcium binding site is discussed further below inthe section “Calcium binding sites.”

Domain B

Domain B, also referred to as loop 3 of the (beta/alpha) 8 barrel, incomprises amino acid residues 133-203 of the amino acid sequence shownin SEQ ID NO: 2. The structure is partially homologous to the structureof Domain B in CGTases, the most striking difference being the presenceof a five amino acid insert corresponding to positions 191-195 in theamino acid sequence shown in SEQ ID NO: 2 which is not found in theCGTases. This insert is spatially positioned close to the active siteresidues and in close contact to the substrate.

Domain C

Domain C in Novamyl comprises amino acid residues 404-496 of the aminoacid sequence shown in SEQ ID NO: 2. Domain C is composed entirely ofβ-strands which form a single 8-stranded sheet structure that folds backon itself, and thus may be described as a β-sandwich structure. One partof the β-sheet forms the interface to Domain A.

Calcium Binding Sites

The structure of the maltogenic alpha-amylase exhibits threecalcium-binding sites; that is, three calcium ions are found to bepresent in the structure. In common with most of the known family 13structures, one calcium ion, WAT 693 in Appendix 1, is located betweenthe A and B domains. This calcium ion is coordinated by a backbonecarbonyl atom from GIn184 and His232, sidechain atoms OD2 and OD1 fromAsp198, a sidechain atom OD1 from Asn131, and three water molecules WATV1, WAT V5 and WAT V8.

A second calcium ion is located in the A domain and is common toCGTases, but not found in α-amylases. The calcium ion WAT 694 iscoordinated by a backbone carbonyl atom from Gly48 and Asp23, sidechainatom OD2 from Asp50, a sidechain atom OD1 from Asp21, a sidechain atomOD1 from Asn26, and a sidechain atom OD1 from Asn27, and one watermolecule WAT V62.

The third calcium ion is located in the A Domain and is unique toNovamyl. The calcium ion is WAT 692 and the coordination comprises abackbone carbonyl atom from Asn77, sidechain atom OE2 and OE1 fromGlu102, a sidechain atom OD1 from Asp79, a sidechain atom OD1 fromAsp76, and a sidechain atom OE1 from Glu101, and one water molecule WATV21.

Substrate Binding Site

Parts of the loop discussed above in the context of domains A and B areof particular interest for substrate interaction and active sitereactivity. In particular, in domain A, residues 37-45 in loop 1,residues 261-266 in loop 5, residues 327-330 in loop 7 and residues370-376 in loop 8; in domain B, residues 135-145 in loop 3, residues173-180 and 188-196 in loop 3, wherein residue positions correspond tothe amino acids in the amino acid sequence in SEQ ID NO: 2.

Without being limited to any theory, it is presently believed thatbinding between a substrate and an enzyme is supported by favorableinteractions found within a sphere of 4 to 6 Å between the substratemolecule and the enzyme, such as hydrogen bonds and/or strongelectrostatic interaction. The following residues of Novamyl (SEQ ID NO:2), are within a distance of 6 Å of the substrate HEX and thus believedto be involved in interactions with said substrate: 44, 89, 90, 92, 93,127, 129, 132, 135, 177, 178, 188, 191, 194, 196, 226, 228, 229, 230,231, 232, 256, 258-261, 288, 328, 329, 371, 372, 373, 376, and 690.

The following residues of Novamyl are within a distance of 4 Å of thesubstrate HEX and thus believed to be involved in interactions with saidsubstrate: 90, 92, 93, 129, 132, 177, 188, 189, 190, 191, 196, 226, 228,229, 231, 232, 256, 258, 259, 260, 261, 328, 329, 372, 376, and 690.

Homology Building of Novamyl®

The structure of the Novamyl® was model built on the structure disclosedin Appendix 1 herein. The structure of other maltogenic alpha-amylasesmay be built analogously.

A model structure of a maltogenic alpha-amylase can be built using theHomology program or a comparable program, eg., Modeller (both fromMolecular Simulations, Inc., San Diego, Calif.). The principle is toalign the sequence of the maltogenic alpha-amylase with the knownstructure with that of the maltogenic alpha-amylase for which a modelstructure is to be constructed. The structurally conserved regions canthen be built on the basis of consensus sequences. In areas lackinghomology, loop structures can be inserted, or sequences can be deletedwith subsequent bonding of the necessary residues using, e.g., theprogram Homology. Subsequent relaxing and optimization of the structureshould be done using either Homology or another molecular simulationprogram, e.g., CHARMm from Molecular Simulations.

Methods for Designing Novel Maltogenic Alpha-Amylase Variants

In a first aspect, the invention relates to a method of constructing avariant of a parent maltogenic alpha-amylase, wherein said variant hasat least one altered property as compared to said parent α-amylase,which method comprises:

i) analyzing the structure of the maltogenic alpha-amylase to identifyat least one amino acid or structural region of said α-amylase, which,on the basis of structural or functional considerations, is determinedto be of relevance for altering said property of the parent maltogenicalpha-amylase;

ii) constructing a variant of the maltogenic alpha-amylase, which ascompared to the parent, has been modified in the amino acid residue orstructural region identified in i) has been modified so as to alter saidproperty; and

iii) testing the resulting variant for said property.

The structural part which is identified in step i) of the method of theinvention may be composed of one amino acid residue. However, normallythe structural part comprises more than one amino acid residue,typically constituting one of the above parts of the maltogenicalpha-amylase structure such as one of the A, B, C, D or E domains, aninterface between any of these domains, a calcium binding site, a loopstructure, the substrate binding site, or the like.

The structural or functional considerations may involve an analysis ofthe relevant structure or structural part and its contemplated impact onthe function of the enzyme. For example, an analysis of the functionaldifferences between maltogenic alpha-amylase and the various CGTases maybe used for assigning certain properties of Novamyl to certain parts ofthe Novamyl structure or to contemplate such relationship. For instance,differences in the pattern or structure of loops surrounding the activesite may result in differences in access to the active site of thesubstrate and thus differences in substrate specificity and/or cleavagepattern.

Furthermore, parts of a maltogenic alpha-amylase involved in substratebinding, and thus, for example, substrate specificity and/or cleavage,calcium ion binding, important, for example, for the calcium dependencyof the enzyme, and the like, have been identified (vide infra).

The modification of an amino acid residue or structural region istypically accomplished by suitable modifications of a DNA sequenceencoding the parent enzyme in question. The modification may besubstitution, deletion or insertion of an amino acid residue or astructural part.

The property to be modified may be stability (e.g. thermostability), pHdependent activity, substrate specificity, specific activity or abilityto reduce retrogradation of starch or staling of bread. Thus, thealtered property may be an altered specific activity at a given pHand/or an altered substrate specificity, such as an altered pattern ofsubstrate cleavage or an altered pattern of substrate inhibition.

In step ii) of the method according to the invention the part of thestructure to be identified is preferably one which in the folded enzymeis believed to be in contact with the substrate (cf, the disclosureabove in the section entitled “Substrate Binding Site”) or involved insubstrate specificity and/or cleavage pattern, and/or one which is incontact with one of the calcium ions and/or one, which is contributingto the pH or temperature profile of the enzyme, or is otherwiseresponsible for the properties of the maltogenic alpha-amylase.

Described in the following are specific types of variants which havebeen designed by use of the method of the invention.

The variants of the invention may comprise additional modifications inaddition to the modifications described herein. The variants preferablyhave an amino acid having more than 70% identity with SEQ ID NO: 2,preferably more than 80%, particularly more than 90%, especially morethan 95%, e.g. more than 98%.

Maltogenic alpha-amylase variants with altered pH dependent activityprofile The pH dependent activity profile can be changed by changing thepKa of residues within 10 Å of the active site residues of themaltogenic alpha-amylase. Changing the pKa of the active site residuesis achieved, e.g., by changing the electrostatic interaction orhydrophobic interaction between functional groups of amino acid sidechains of a given amino acid residue and its close surroundings. Toobtain a higher activity at a higher pH, negatively charged residues areplaced near a hydrogen donor acid, whereas positively charged residuesplaced near a nucleophilic acid will result in higher activity at lowpH. Also, a decrease in the pKa can be obtained by reducing theaccessibility of water or increasing hydrophobicity of the environment.

Thus, another aspect of the present invention relates to a variant of aparent maltogenic alpha-amylase, in which the variant has an altered pHdependent activity profile as compared to the parent, wherein thevariant may be obtained by the following method:

i) identifying an amino acid residue within 15 Å from an active siteresidue of a maltogenic alpha-amylase in the three-dimensional structureof said parent maltogenic alpha-amylase, in particular 10 Å from anactive site residue, wherein said amino acid residue is contemplated tobe involved in electrostatic or hydrophobic interactions with an activesite residue;

ii) substituting, in the structure, said amino acid residue with anamino acid residue which changes the electrostatic and/or hydrophobicsurroundings of an active site residue, and evaluating the accommodationof the amino acid residue in the structure,

iii) optionally repeating step i) and/or ii) recursively until an aminoacid substitution has been identified which is accommodated into thestructure,

iv) constructing a maltogenic alpha-amylase variant resulting from stepsi) and ii), and optionally iii), and testing the pH dependent enzymaticactivity of said variant.

In a preferred embodiment, the variant of a maltogenic alpha-amylasehaving an altered pH dependent activity profile as compared to theparent maltogenic alpha-amylase comprises a modification of an aminoacid residue corresponding to one or more of the following residues ofthe amino acid sequence set forth in SEQ ID NO: 2: D127, V129, F188,A229, Y258, V281, F284, T288, N327, M330, G370, N371, and D372, L71,S72, V74, L75, L78, T80, L81, G83, T84, D85, N86, T87, G88, Y89, H90,G91, T94, R95, D96, F97, I174, S175, N176, D178, D179, R180, Y181, E182,A183, Q184, K186, N187, F188, T189, D190, A192, G193, F194, S195, L196.

In more preferred embodiment, the variant comprises a modificationcorresponding to one or more of the following modifications in the aminoacid sequence set forth in SEQ ID NO: 2: D127N/L, V129S/T/G/V,F188E/K/H, A229S/T/GN, Y258E/D/K/R/F/N, V281L/T, F284K/H/D/EN,T288E/K/R, N327D, M330L/F/I/D/E/K, G370N,N371 D/E/G/K, and D372N/V,L711, S72C, V741, L75N/D/Q/I/V, L78N/I, T80I/L/V/S/N/G,L811N/S/T/N/Q/K/H, G83A/S/T/N/Q/E/D/R/H/L, T84S/A/N/D/G, D85A/T/S/N/G,N86Q/E/D/Y/H/K, T87511, G88A/S/T, Y89F, H90N/Q/K, G91A/S/T,T94N/D/A/M/V/I, R95K/Q, D96N/V/Q/I, F97Y, 1174N/Q/L, S175T/A/N/D,N176S/T/H/Q/P, D178N/Q/E/K/H, D179Y/N/H, R180W, Y181R/F/C/L, E1 82D,A183S/C/G, Q184E, K186R, N187Q/E/L/F/H/K/V/L, F188Y/L/I/H/N,T189N/D/A/S/H/Y/G, D190E/Q/H/N/K, A192T/D/E/N/K, G193A/S/T, F194Y,S195N/D/E/R/K/G, L1961.

Similar modifications may be introduced in equivalent positions of othermaltogenic alpha-amylases. Variants of particular interest have acombination of one or more of the above with any of the othermodifications disclosed herein.

Maltogenic Alpha-Amylase Variants with Altered Stability

A variant with improved stability (typically increased stability) may beobtained by stabilization of calcium binding, substitution with proline,substitution of histidine with another amino acid, introduction of aninterdomain disulfide bond, removal of a deamidation site, altering ahydrogen bond contact, filling in an internal structural cavity with oneor more amino acids with bulkier side groups, introduction ofinterdomain interactions, altering charge distribution, helix capping,or introduction of a salt bridge.

Calcium Binding

The invention provides a variant of a parent maltogenic alpha-amylase,which has an altered stability due to an altered stabilization ofcalcium (Ca²⁺) binding. The enzyme variant may have alteredthermostability or pH dependent stability, or it may have maltogenicalpha-amylase activity in the presence of a lower concentration ofcalcium ion. It is presently believed that amino acid residues locatedwithin 10 Å from a calcium ion are involved in or are of importance forthe Ca²⁺ binding capability of the enzyme.

The amino acid residues found within a distance of 10 Å from the Ca²⁺binding sites of the maltogenic alpha-amylase with the amino acidsequence set forth in SEQ ID NO: 2 were determined as described inExample 2 and are as follows: 16, 17, 18, 19, 20, 21, 22, 23, 24, 25,26, 27, 28 29, 30, 31, 32, 33, 35, 36, 40, 46, 47, 48, 49, 50, 51, 52,53, 54, 56, 73, 74, 75, 76, 77, 78, 79, 80, 81, 87, 88, 89, 91, 93, 94,95, 96, 99, 100, 101, 102, 103, 104, 105, 109, 129, 130, 131, 132, 133,134, 145, 150, 167, 168, 169, 170, 171, 172, 174, 177, 180, 181, 182,183, 184, 185, 186, 187, 188, 189, 196, 197, 198, 199, 200, 201, 202,206, 210, 228, 229, 230, 231, 232, 233, 234, 235, 237, 378, and 637.

In order to construct a variant according to this aspect of theinvention it is desirable to substitute at least one of the abovementioned amino acid residues, which is determined to be involved in anon-optimal calcium binding, with any other amino acid residue whichimproves the Ca²⁺ binding affinity of the variant enzyme. Accordingly,another aspect of the invention relates to a method of constructing avariant of a parent maltogenic alpha-amylase wherein said variant has astabilised Ca²⁺ binding as compared to said parent, which methodcomprises:

i) identifying an amino acid residue within 10 Å from a Ca²⁺ bindingsite of a maltogenic alpha-amylase in a model of the three-dimensionalstructure of said α-amylase which, from structural or functionalconsiderations, is determined to be responsible for a non-optimalcalcium ion interaction;

ii) constructing a variant in which said amino acid residue issubstituted with another amino acid residue which, from structural orfunctional considerations, is determined to be important forestablishing an altered Ca²⁺ binding affinity; and

iii) testing the Ca²⁺ binding of the resulting maltogenic alpha-amylasevariant.

Substituting an amino acid residue responsible for non-optimal calciumion interaction with another residue may alter a calcium ion bindinginteraction of the enzyme. For instance, the amino acid residue inquestion may be selected on the basis of one or more of the followingobjectives:

a) to obtain an improved interaction between a calcium ion and an aminoacid residue as identified from the structure of the maltogenicalpha-amylase. For instance, if the amino acid residue in question isexposed to a surrounding solvent, it may be advantageous to increase theshielding of said amino acid residue from the solvent so as to stabilizethe interaction between said amino acid residue and a calcium ion. Thiscan be achieved by substituting said residue, or an amino acid residuein the vicinity of said residue contributing to the shielding, with anamino acid residue with a bulkier side group or which otherwise resultsin an improved shielding effect.

b) to stabilize a calcium binding site, for instance by stabilizing thestructure of the maltogenic alpha-amylase, e.g. by stabilizing thecontacts between two or more of the five domains or stabilizing one ormore of the individual domains as such. This may, e.g., be achieved byproviding for a better coordination to amino acid side chains, whichmay, e.g., be obtained by substituting an N residue with a D residueand/or a Q residue with an E residue, e.g. within 10 Å, and preferablywithin 3 or 4 Å, of a calcium binding site.

c) to improve the coordination between the calcium ion and the calciumbinding residues, e.g., by improving the interaction between the ion andthe coordinating residues or increasing the number of sidechaincoordinations by substituting a coordinating water with an amino acidsidechain.

d) replace water by a coordinating calcium amino acid residue.

Preferably, the amino acid residue to be modified is located within 8 Åof a Ca²⁺ ion, preferably within 5 Å of a Ca²⁺ ion. The amino acidresidues within 8 Å and 5 Å, respectively, may easily be identified byan analogous method used for identifying amino acid residues within 10 Å(cf. Example 2)

In a preferred embodiment, the variant of a maltogenic alpha-amylasehaving an altered Ca²⁺ binding as compared to the parent maltogenicalpha-amylase comprises a substitution of an amino acid residuecorresponding to one or more of the following residues of the amino acidsequence set forth in SEQ ID NO: 2:

D17, A30, S32, R95, H103, N131, Q201, I174, and/or H169, V74, L75, L78,T80, L81, T87, G88, Y89, H90, G91, T94, R95, D96, F97, Y167, F168, H169,H170, N171, G172, D173, I174, S175, N176, D178, D179, R180, Y181, E182,A183, Q184, K186, N187, F188, T189.

In more preferred embodiment, the variant of a maltogenic alpha-amylasecomprises a substitution corresponding to one or more of the followingsubstitutions in the amino acid sequence set forth in SEQ ID NO: 2:

D17E/Q, A30M/L/A/V/I/E/Q, S32D/E/N/Q, R95M/L/A/V/I/E/Q, H103Y/N/Q/D/E,N131 D, Q201 E, I174E/Q, and H169N/D/E/Q V74I, L75N/D/Q/I/V, L78N/I,T80I/L/V/S/N/G, L81I/N/S/T/N/Q/K/H, T87S/I, G88A/S/T, Y89F, H90N/Q/K,G91A/S/T, T94N/D/A/M/V/I, R95K/Q, D96N/V/Q/I, F97Y, Y167F/R/C, F168Y,H169 N/Q/K, H170 N/Q/K, N171D/E/Q/H/R/K/G, G172A/T/S, D173 N/S/T/Y/R/G,I174 N/Q/L, S175T/A/N/D, N176S/T/H/Q/P, D178N/Q/E/K/H, D179Y/N/H, R180W,Y181R/F/C/L, E182D, A183S/C/G, Q184E, K186R, N187Q/E/L/F/H/K/V/L,F188Y/L/I/H/N, T189N/D/A/S/H/Y/G.

In another preferred embodiment of the invention with respect toaltering the Ca²⁺ binding of a maltogenic alpha-amylase the partialsequence N28-P29-A30-K31-S32-Y33-G34 as set forth in SEQ ID NO: 2 ismodified.

Similar substitutions may be introduced in equivalent positions of othermaltogenic alpha-amylases. Modifications of particular interest are anycombination of one or more of the above with any of the othermodifications disclosed herein.

Other Substitutions

Variants with improved stability of the enzyme can be achieved byimproving existing or introducing new interdomain and intradomaincontacts. Such improved stability can be achieved by the modificationslisted below.

The maltogenic alpha-amylase having the amino acid sequence shown in SEQID NO: 2 may be stabilized by the introduction of one or moreinterdomain disulfide bonds. Accordingly, another preferred embodimentof the present invention relates to a variant of a parent maltogenicalpha-amylase which has improved stability and at least one moreinterdomain disulfide bridge as compared to said parent, wherein saidvariant comprises a modification in a position corresponding to at leastone of the following pairs of positions in SEQ ID NO: 2:

G236+S583, G618+R272, T252+V433 and/or A348+V487.

In a more preferred embodiment, the substitution corresponds to at leastone of the following pairs:

G236C+S583C, G618C+R272c, T252C+V433C and/or A348C+V487C.

Another preferred embodiment of the invention relates to a variant of aparent maltogenic alpha-amylase which has an improved stability and analtered interdomain interaction as compared to said parent, wherein saidvariant comprises a substitution in a position corresponding at leastone of the following sets of positions in SEQ ID NO: 2:

i) F143, F194, L78;

ii) A341, A348, L398, I415, T439, L464, L465; iii) L557;

iv) S240, L268;

v) Q208, L628;

vi) F427, Q500, N507, M508, S573; and

vii) I510, V620.

In a more preferred embodiment, the substitution corresponds to at leastone of the following sets:

i) F143Y, F194Y, L78Y/F/W/E/Q;

ii) A341S/D/N, A348V/I/L, L398E/Q/N/D, I415E/Q, T439D/E/Q/N, L464D/E,L465D/E/N/Q/R/K;

iii) L557Q/E/N/D;

iv) S240D/E/N/Q, L268D/E/N/Q/R/K;

v) Q208D/E/Q, L628E/Q/N/D;

vi) F427E/Q/R/K/Y, Q500Y, N507Q/E/D, M508K/R/E/Q, S573D/E/N/Q; and/or

vii) 1510D/E/N/Q/S, V620D/E/N/Q.

Another preferred embodiment of the invention relates to a variant of aparent maltogenic alpha-amylase which has an improved stability and oneor more salt bridges as compared to said parent, wherein said variantcomprises a substitution in a position corresponding at least one of thefollowing sets of positions in SEQ ID NO: 2:

N106, N320 and Q624.

In a more preferred embodiment, the variant of a maltogenicalpha-amylase comprises a substitution corresponding to the followingsubstitutions in the amino acid sequence set forth in SEQ ID NO: 2:

N106R, N320E/D and/or Q624E.

Another embodiment of the invention relates to a variant of a parentmaltogenic alpha-amylase which has an improved stability and whereinsaid variant comprises a substitution in a position corresponding atleast one of the following sets of positions in SEQ ID NO: 2:

K40, V74, S141, T142, F188, N234, K249, D261, D261, L268, V279, N342,G397, A403, K425, S442, S479, S493, T494, S495, A496, S497, A498, Q500,K520, A555 and N595.

In a more preferred embodiment, the variant of a maltogenicalpha-amylase comprises a substitution corresponding to one or more ofthe following substitutions with proline in the amino acid sequence setforth in SEQ ID NO: 2:

V74P, S141P, N234P, K249P, L268P, V279P, N342P, G397P, A403P, S442P,S479P, S493P, T494P, S495P, A496P, S497P, A498P, Q500P, and/or A555P.

Other preferred substitutions are K40R, T142A, F188I/L, D261G, K425E,K520R, and/or N595I.

Analogously, it may be preferred that one or more histidine residuespresent in the parent maltogenic alpha-amylase is or are substitutedwith a non-histidine residues such as Y, V I, L, F, M, E, Q, N, or D.Accordingly, in another preferred embodiment, the variant of amaltogenic alpha-amylase comprises a substitution of an amino acidresidue corresponding to one or more of the following residues of theamino acid sequence set forth in SEQ ID NO: 2: H103, H220, and H344

In a more preferred embodiment, the variant of a maltogenicalpha-amylase comprises a substitution corresponding to one or more ofthe following substitutions in the amino acid sequence set forth in SEQID NO: 2:

H103Y/V/I/L/F/Y, H220Y/L/M, and H344E/Q/N/D/Y.

It may be preferred that one or more asparagine or glutamine residuespresent in the parent maltogenic alpha-amylase is or are substitutedwith a residue lacking the amide on the side chain. Accordingly, inanother preferred embodiment, the variant of a Novamyl-like comprises asubstitution of an amino acid residue corresponding to one or more ofthe following residues of the amino acid sequence set forth in SEQ IDNO: 2: Q13, N26, N77, N86, N99, Q119, N120, N131, N152, N171, N176,N187, Q201, N203, N234, Q247, N266, N275, N276, N280, N287, Q299, N320,N327, N342, Q365, N371, N375, N401, N436, N454, N468, N474, Q500, N507,N513, Q526, N575, Q581, N621, Q624 and N664.

In more preferred embodiment, the variant of a maltogenic alpha-amylasecomprises a substitution corresponding to one or more of the followingsubstitutions in the amino acid sequence set forth in SEQ ID NO: 2:

Q13S/T/A/V/L/I/F/M, N26S/T/A/V/L/I, N77S/T/A/V/L/I, N86S/T/A/V/L/I,N99T/S/V/L, Q119T/S, N120S/T/A/V/L/I, N131S/T/A/V/L/I, N152T/S/V/L,N171Y/D/S/T, N176S/T/A/V/L/I, N187S/T/A/V/L/I, Q201S/T/A/V/L/I/F/M,N203D/S/T/A/V/L/I, N234S/T/A/V/L/I, Q247S/T/A/V/L/I/F/M,N266S/T/A/V/L/I, N275S/T/A/V/L/I, N276S/T/A/V/L/I, N280S/T/A/V/L/I,N287S/T/A/V/L/I, Q299L/T/S, N320S/T/A/V/L/I, N327S/T/A/V/L/I,N342S/T/A/V/L/I, Q365S/T/A/V/L/I, N371S/T/A/V/L/I, N375S/T/A/V/L/I,N401S/T/A/V/L/I, N436S/T/A/V/L/I, N454D/S/T/A/V/L/I, N468D/S/T/A/V/L/I,N474D/S/T/A/V/L/I, Q500S/T/A/V/L/I/F/M, N507S/T/A/V/L/I,N513S/T/A/V/L/I, Q526 D/S/T/A/V/L/I, N575S/T/A/V/L/I,Q581S/T/A/V/L/I/F/M, N621S/T/A/V/L/I Q624S/T/A/V/L/I/F/M andN664D/S/T/A/V/L/I.

Another embodiment of the invention relates to a variant of a parentmaltogenic alpha-amylase which has improved stability and improvedhydrogen bond contacts as compared to said parent, wherein said variantcomprises a modification in a position corresponding to one or more ofthe following positions in SEQ ID NO: 2: I16, L35, M45, P73, D76, D79,A192, I100, A148, A163+G172, L268, V281, D285, L321, F297, N305, K316,S573, A341, M378, A381, F389, A483, A486, I510, A564, F586, K589, F636,K645, A629, and/or T681.

In a preferred embodiment, the modification corresponds to one or moreof the following:

I16T/D/N, L35Q, M45K, P73Q, D76E, D79EN, A192S/D/N, 1100T/S/D/N/E/Q,A148D/N/E/Q/S/T/R/K, A163Y+G172S/D/N, L268R/K, V281/Q, D285R/K, L321Q,F297N/D/Q/E, N305K/R, K316N/D, S573N/D, A341R/K, M378R/K, A381S/D/N,F389Y, A483S/D/N, A486Q/E, I510R/K, A564S/D/N, F586S/D/N, K589S/D/Q/N,F636Y, K645T, A629N/D/E/Q, and/or T681D/N/E/Q/S.

Similar substitutions may be introduced in equivalent positions of othermaltogenic alpha-amylases. Substitutions of particular interest are anycombination of one or more of the above with any of the othermodifications disclosed herein.

Before actually constructing a maltogenic alpha-amylase variant toachieve any of the above objectives, it may be convenient to evaluatewhether or not the contemplated amino acid modification can beaccommodated into the maltogenic alpha-amylase structure, e.g. into amodel of the three-dimensional structure of the parent maltogenicalpha-amylase.

Maltogenic Alpha-Amylase Variants with Altered Thermostability and/orAltered Temperature Dependent Activity Profile

The invention further relates to a variant of a parent maltogenicalpha-amylase, which results from substitution, deletion or insertion ofone or more amino acid residues so as to obtain a variant having analtered thermostability or temperature dependent activity profile.

The structure of the maltogenic alpha-amylase contains a number ofunique internal cavities which may contain water and a number ofcrevices. In order to increase the thermostability of the polypeptide itmay be desirable to reduce the number or size of cavities and crevices,e.g., by introducing one or more hydrophobic contacts, preferablyachieved by introducing amino acids with bulkier side groups in thevicinity or surroundings of the cavity. For instance, the amino acidresidues to be modified are those which are involved in the formation ofthe cavity.

Accordingly, in a further aspect the present invention relates to amethod of increasing the thermostability and/or altering the temperaturedependent activity profile of a parent maltogenic alpha-amylase, whichmethod comprises:

i) identifying an internal cavity or a crevice of the parent maltogenicalpha-amylase in the three-dimensional structure of said polypeptide;

ii) substituting, in the structure, one or more amino acid residues inthe neighbourhood of the cavity or crevice identified in step i) withanother amino acid residue which, from structural or functionalconsiderations, is determined to increase the hydrophobic interactionand to fill out or reduce the size of the cavity or crevice; and

iii) constructing a variant of the parent maltogenic alpha-amylaseresulting from step ii) and testing the thermostability and/ortemperature dependent activity of the variant.

The structure identified in Appendix 1 may be used for identifying thecavity or crevice of the parent maltogenic alpha-amylase.

It will be understood that the cavity or crevice is identified by theamino acid residues surrounding said cavity or crevice, and thatmodification of said amino acid residues are of importance for fillingor reducing the size of said cavity or crevice. Preferably, themodification is a substitution with a bulkier amino acid residue, i.e.one with a greater side chain volume. For example, all the amino acidsare bulkier than Gly, whereas Tyr and Trp are bulkier than Phe. Theparticular amino acid residues referred to below are those which in acrystal structure have been found to flank the cavity or crevice inquestion.

In a preferred embodiment, the variant of a maltogenic alpha-amylase, inorder to fill, either completely or partly, cavities located internallyin the structure, comprises a substitution of an amino acid residuecorresponding to one or more of the following residues of the amino acidsequence set forth in SEQ ID NO: 2:

L51, L75, L78, G88, G91, T94, V114, I125, V126, T134, G157, L217, S235,G236, V254, V279, V281, L286, V289, I290, V308, L321, I325, D326, L343,F349, S353, I359, I405, L448, Q449, L452, I470, G509, V515, S583, G625,L627, L628 and A670.L71, S72, V74, L75, L78, T80, L81, G83, T84, D85, N86, T87, G88, Y89,H90, G91, T94, R95, D96, F97, Y167, F168, H169, H170, N171, G172, D173,I174, S175, N176, D178, D179, R180, Y181, E182, A183, Q184, K186, N187,F188, T189, D190, A192, G193, F194, S195, L196.

In a more preferred embodiment, the variant of a maltogenicalpha-amylase comprises one or more substitutions corresponding to thefollowing substitutions in the amino acid sequence set forth in SEQ IDNO: 2:

L217 in combination with L75 (e.g. L217F/Y in combination with L75F/Y),L51W, L75F/Y, L781, G88A/V/T, G91T/S/V/N, T94V/I/L, V114V/I/L,I125L/M/F/Y/W, V1261/L, T134V/I/L/M/F/Y/W, G157A/V/I/L, L217V/I/M/F/Y/W,S235I/L/M/F/Y/W, G236A/V/I/L/M/F/Y/W, V254I/L/M/F/Y/W, V279M/I/L/F,V281I/L/M/F/Y/W, L286F, V289I/L/R, I290M/L/F, V308I/L/M/F/Y/W,L321I/M/F/Y/W, I325L/M/F/Y/W, D326E/Q, L343M/F/Y/W, F349W/Y, S353V/I/L,I359L/M/F/Y/W, I405M/L/Y/F/W, L448Y, Q449Y, L452M/Y/F/W, I470M/L/F,G509A/V/I/L/M/S/T/D/N, V515I/L, S583V/I/L/V, G625A/V/I/L/M/F/Y/W,L627M/F/Y, L628M/I/F/Y/W and A670V/I/L/M/F/Y/W, L71I, S72C, V74I,L75N/D/Q/I/V, L78N/I, T80I/L/V/S/N/G, L811N/S/T/N/Q/K/H,G83A/S/T/N/Q/E/D/R/H/L, T84S/A/N/D/G, D85A/T/S/N/G, N86Q/E/D/Y/H/K,T87S/I, G88A/S/T, Y89F, H90N/Q/K, G91A/S/T, T94N/D/A/M/V/I, R95K/Q,D96N/V/Q/I, F97Y, Y167F/R/C, F168Y, H169 N/Q/K, H170 N/Q/K,N171D/E/Q/H/R/K/G, G172A/T/S, D173 N/S/TN/R/G, I174 N/Q/L, S175T/A/N/D,N176S/T/H/Q/P, D178N/Q/E/K/H, D179Y/N/H, R180W, Y181R/F/C/L, E182D,A1835/C/G, Q184E, K186R, N187Q/E/L/F/H/K/V/L, F188Y/L/I/H/N,T189N/D/A/S/H/Y/G, D190E/Q/H/N/K, A192T/D/E/N/K, G193A/S/T, F194Y,S195N/D/E/R/K/G, L1961.

Similar substitutions may be introduced in equivalent positions of othermaltogenic alpha-amylases. Variants of particular interest have acombination of one or more of the above with any of the othermodifications disclosed herein.

Maltogenic Alpha-Amylase Variants with an Altered Cleavage Pattern

One aim of the present invention is to change the degradationcharacteristics of a maltogenic alpha-amylase. Thus, Novamyl hydrolyzesstarch to form predominantly maltose (G2) and a small amount of glucose(G1), but virtually no higher oligosaccharides (G3+). It may bedesirable to change this cleavage pattern, e.g. so as to form higheramounts of higher oligosaccharides, such as maltotriose (G3),maltotetraose (G4) and maltopentaose (G5).

A variant of a parent maltogenic alpha-amylase in which the substratecleavage pattern is altered as compared to said parent may beconstructed by a method which comprises:

i) identifying the substrate binding area of the parent maltogenicalpha-amylase in a model of the three-dimensional structure, e.g. withina sphere of 4 Å from the substrate binding site as defined in thesection above entitled “Substrate Binding Site”;

ii) substituting in the model one or more amino acid residues of thesubstrate binding area of the cleft identified in i) which is or arebelieved to be responsible for the cleavage pattern of the parent withanother amino acid residue which from structural or functionalconsiderations is believed to result in an altered substrate cleavagepattern, or deleting one or more amino acid residues of the substratebinding area contemplated to introduce favorable interactions to thesubstrate or adding one or more amino acid residues to the substratebinding area contemplated to introduce favorable interactions to thesubstrate; and

iii) constructing a maltogenic alpha-amylase variant resulting from stepii) and testing the substrate cleavage pattern of the variant.

Accordingly, another aspect of the invention relates to a variant of aparent maltogenic alpha-amylase which has an altered substrate bindingsite as compared to said parent, which variant comprises a modificationin a position corresponding to one or both of the following positions inSEQ ID NO: 2:

V281 and/or A629.

In a preferred embodiment, the variant comprises a modificationcorresponding to: V281Q and/or A629N/D/E/Q.

Similar modifications may be introduced in equivalent positions of othermaltogenic alpha-amylases. Substitutions of particular interest are anycombination of one or both of the above with any of the othermodifications disclosed herein.

Maltogenic Alpha-Amylase Variants with Improved Ability to ReduceRetrogradation of Starch and/or Staling of Bread

The invention provides maltogenic alpha-amylase variants having improvedability to reduce the retrogradation of starch and/or the staling ofbread. Preferred variants comprise a modification at one or morepositions corresponding to the following amino acid residues in SEQ IDNO: 2:

A30, K40, N115, T142, F188, T189, P191, A192, G193, F194, S195, D261,N327, K425, K520 and N595.

In a more preferred embodiment, the variant comprises one or moremodifications corresponding to the following in SEQ ID NO: 2:

A30D, K40R, N115D, T142A, F188L, T189Y, A (191-195), D261G, D261G,N327S, K425E, K520R and N5951.

Determination of Residues within 10 Å from Calcium Ions

The coordinates of Appendix 1 are read into the INSIGHT program (BIOSYMTechnologies). The spatial coordinates are presented showing the bondsbetween the atoms. The ions are presented as well as the water atoms.The part of the program package for creating subsets was used to createa 10 Å subset around the calcium ions in the structure by using thecommand ZONE. All residues identified as having an atom within thedesignated 10 Å distance from a calcium ion are compiled and listed byusing the command LIST MOLECULE. By giving the ions the name “VAT CA” inthe coordinate file, a 10 Å sphere around all atoms called “VAT CA” iscompiled. The specific residues identified in this manner are givenfurther above in the section entitled “Calcium binding”.

Determination of Cavities

The solved structure of Novamyl with the structural coordinates setforth in Appendix 1 reveals many internal crevices and cavities. Whenanalysing for such cavities the Connolly program is normally used (Lee,B. and Richards, F. M. (1971) J. Mol. Biol. 55:379-400). The programuses a probe with radius to search the external and internal surface ofthe protein. The smallest crevice observable in this way has the proberadius.

To analyse the solved structure a modified version of the Connollyprogram included in the program of INSIGHT was used. In the first step,the water molecules and the ions were removed by unmerging these atomsfrom the solved structure. By using the command MOLECULE SURFACE SOLVENTthe solvent accessible surface area was calculated for all atoms andresidues using a probe radius of 1.4 Å, and displayed graphicallytogether with the model of the solved structure. The internal cavitiesare then seen as dot surfaces with no connections to the externalsurface.

Suggestions for specific modifications to fill out the cavities aregiven above in the section entitled “Variants with alteredthermostability and/or altered temperature dependent activity profile”).By using the homology built structures or/and comparisons based onsequence alignment, mutations for homologous structures of maltogenicalpha-amylases can be made.

Nomenclature for Amino Acid Modifications

The nomenclature used herein for defining mutations is essentially asdescribed in WO 92/05249. Thus, F188H indicates a substitution of theamino acid F (Phe) in position 188 with the amino acid H(His).V129S/T/G/V indicates a substitution of V129 with S, T, G or V. A(191-195) or A (191-195) indicates a deletion of amino acids inpositions 191-195. 192-A-193 indicates an insertion of A between aminoacids 192 and 193.

Polypeptide Sequence Identity

For purposes of the present invention, the degree of identity may besuitably determined according to the method described in Needleman, S.B. and Wunsch, C. D., (1970), Journal of Molecular Biology, 48, 443-45,with the following settings for polypeptide sequence comparison: GAPcreation penalty of 3.0 and GAP extension penalty of 0.1. Thedetermination may be done by means of a computer program known such asGAP provided in the GCG program package (Program Manual for theWisconsin Package, Version 8, August 1994, Genetics Computer Group, 575Science Drive, Madison, Wis., USA 53711).

The variants of the invention have an amino acid identity with aminoacids 1-686 of SEQ ID NO: 2 of at least 70%, preferably at least 80%,e.g. at least 90%, particularly at least 95% or at least 98%.

Hybridization

Suitable experimental conditions for determining hybridization between anucleotide probe and a homologous DNA or RNA sequence involvespresoaking of the filter containing the DNA fragments or RNA tohybridize in 5× SSC (sodium chloride/sodium citrate, Sambrook, et al.,1989) for 10 min, and prehybridization of the filter in a solution of 5×SSC, 5×Denhardt's solution (Sambrook, et al., 1989), 0.5% SDS and 100μg/ml of denatured sonicated salmon sperm DNA (Sambrook, et al., 1989),followed by hybridization in the same solution containing arandom-primed (Feinberg, A. P. and Vogelstein, B. (1983) Anal. Biochem.132:6-13), ³²P-dCTP-labeled (specific activity>1×10⁹ cpm/μg) probe for12 hours at ca. 45° C. The filter is then washed twice for 30 minutes in2× SSC, 0.5% SDS at least 55° C. (low stringency), preferably at least60° C. (medium stringency), more preferably at least 65° C. (medium/highstringency), more preferably at least 70° C. (high stringency), evenmore preferably at least 75° C. (very high stringency).

Molecules which hybridize to the oligonucleotide probe under theseconditions are detected by exposure to x-ray film.

Methods of Preparing Variants of Maltogenic Alpha-Amylases Cloning a DNASequence Encoding a Novamyl-Like Polypeptide

The DNA sequence encoding a parent maltogenic alpha-amylase may beisolated from any cell or microorganism producing the maltogenicalpha-amylase in question, using various methods well known in the art,for example, from the Bacillus strain NCIB 11837.

First, a genomic DNA and/or cDNA library should be constructed usingchromosomal DNA or messenger RNA from the organism that produces themaltogenic alpha-amylase to be studied. Then, if the amino acid sequenceof the α-amylase is known, homologous, labelled oligonucleotide probesmay be synthesised and used to identify maltogenicalpha-amylase-encoding clones from a genomic library prepared from theorganism in question. Alternatively, a labelled oligonucleotide probecontaining sequences homologous to a known α-amylase gene could be usedas a probe to identify maltogenic alpha-amylase-encoding clones, usinghybridization and washing conditions of lower stringency.

Another method for identifying maltogenic alpha-amylase-encoding clonesinvolves inserting fragments of genomic DNA into an expression vector,such as a plasmid, transforming α-amylase negative bacteria with theresulting genomic DNA library, and then plating the transformed bacteriaonto agar containing a substrate for maltogenic alpha-amylase, therebyallowing clones expressing maltogenic alpha-amylase activity to beidentified.

Alternatively, the DNA sequence encoding the enzyme may be preparedsynthetically by established standard methods, e.g. the phosphoroamiditemethod described by S. L. Beaucage and M. H. Caruthers (1981) or themethod described by Matthes et al. (1984). In the phosphoroamiditemethod, oligonucleotides are synthesized, e.g. in an automatic DNAsynthesizer, purified, annealed, ligated and cloned in appropriatevectors.

Finally, the DNA sequence may be of mixed genomic and synthetic origin,mixed synthetic and cDNA origin or mixed genomic and cDNA origin,prepared by ligating fragments of synthetic, genomic or cDNA origin,wherein the fragments correspond to various parts of the entire DNAsequence, in accordance with techniques well known in the art. The DNAsequence may also be prepared by polymerase chain reaction (PCR) usingspecific primers, for instance as described in U.S. Pat. No. 4,683,202or R. K. Saiki et al. (1988).

Site-Directed Mutaqenesis

Once a maltogenic alpha-amylase-encoding DNA sequence has been isolated,and desirable sites for modification identified, modifications may beintroduced using synthetic oligonucleotides. These oligonucleotidescontain nucleotide sequences flanking the desired modification sites;mutant nucleotides are inserted during oligonucleotide synthesis. In aspecific method, a single-stranded gap of DNA, bridging the maltogenicalpha-amylase-encoding sequence, is created in a vector carrying themaltogenic alpha-amylase gene. Then the synthetic nucleotide, bearingthe desired modification, is annealed to a homologous portion of thesingle-stranded DNA. The remaining gap is then filled in with DNApolymerase I (Klenow fragment) and the construct is ligated using T4ligase. A specific example of this method is described in Morinaga etal. (1984). U.S. Pat. No. 4,760,025 discloses the introduction ofoligonucleotides encoding multiple modifications by performing minoralterations of the cassette. However, an even greater variety ofmodifications can be introduced at any one time by the Morinaga methodbecause a multitude of oligonucleotides, of various lengths, can beintroduced.

Another method of introducing modifications into a maltogenicalpha-amylase-encoding DNA sequences is described in Nelson and Long(1989). It involves a 3-step generation of a PCR fragment containing thedesired modification introduced by using a chemically synthesized DNAstrand as one of the primers in the PCR reactions. From thePCR-generated fragment, a DNA fragment carrying the modification may beisolated by cleavage with restriction endonucleases and reinserted intoan expression plasmid.

Random Mutaqenesis

Random mutagenesis is suitably performed either as localised orregion-specific random mutagenesis in at least three parts of the genetranslating to the amino acid sequence shown in question, or within thewhole gene.

The random mutagenesis of a DNA sequence encoding a parent maltogenicalpha-amylase may be conveniently performed by use of any method knownin the art.

In relation to the above, a further aspect of the present inventionrelates to a method for generating a variant of a parent Novamyl-likeα-amylase, wherein the variant exhibits increased stability at low pHand at low calcium concentration relative to the parent, the methodcomprising:

(a) subjecting a DNA sequence encoding the parent Novamyl-like α-amylaseto random mutagenesis,

(b) expressing the mutated DNA sequence obtained in step (a) in a hostcell, and

(c) screening for host cells expressing a Novamyl-like α-amylase variantwhich has an altered property relative to the parent Novamyl-likeα-amylase.

Step (a) of the above method of the invention is preferably performedusing doped primers, as described in the working examples herein (videinfra).

For instance, the random mutagenesis may be performed by use of asuitable physical or chemical mutagenizing agent, by use of a suitableoligonucleotide, or by subjecting the DNA sequence to PCR generatedmutagenesis. Furthermore, the random mutagenesis may be performed by useof any combination of these mutagenizing agents. The mutagenizing agentmay, e.g., be one which induces transitions, transversions, inversions,scrambling, deletions, and/or insertions.

Examples of a physical or chemical mutagenizing agent suitable for thepresent purpose include ultraviolet (UV) irradiation, hydroxylamine,N-methyl-N′-nitro-N-nitrosoguanidine (MNNG), O-methyl hydroxylamine,nitrous acid, ethyl methane sulphonate (EMS), sodium bisulphite, formicacid, and nucleotide analogues. When such agents are used, themutagenesis is typically performed by incubating the DNA sequenceencoding the parent enzyme to be mutagenized in the presence of themutagenizing agent of choice under suitable conditions for themutagenesis to take place, and selecting for mutated DNA having thedesired properties.

When the mutagenesis is performed by the use of an oligonucleotide, theoligonucleotide may be doped or spiked with the three non-parentnucleotides during the synthesis of the oligonucleotide at the positionswhich are to be changed. The doping or spiking may be done so thatcodons for unwanted amino acids are avoided. The doped or spikedoligonucleotide can be incorporated into the DNA encoding the maltogenicalpha-amylase enzyme by any published technique, using e.g. PCR, LCR orany DNA polymerase and ligase as deemed appropriate.

Preferably, the doping is carried out using “constant random doping”, inwhich the percentage of wild-type and modification in each position ispredefined. Furthermore, the doping may be directed toward a preferencefor the introduction of certain nucleotides, and thereby a preferencefor the introduction of one or more specific amino acid residues. Thedoping may be made, e.g., so as to allow for the introduction of 90%wild type and 10% modifications in each position. An additionalconsideration in the choice of a doping scheme is based on genetic aswell as protein-structural constraints. The doping scheme may be made byusing the DOPE program which, inter alia, ensures that introduction ofstop codons is avoided.

When PCR-generated mutagenesis is used, either a chemically treated ornon-treated gene encoding a parent maltogenic alpha-amylase enzyme issubjected to PCR under conditions that increase the misincorporation ofnucleotides (Deshler 1992; Leung et al., Technique, Vol. 1, 1989, pp.11-15).

A mutator strain of E. coli (Fowler et al., Molec. Gen. Genet., 133,1974, pp. 179-191), S. cereviseae or any other microbial organism may beused for the random mutagenesis of the DNA encoding the maltogenicalpha-amylase by, e.g., transforming a plasmid containing the parentenzyme into the mutator strain, growing the mutator strain with theplasmid and isolating the mutated plasmid from the mutator strain. Themutated plasmid may be subsequently transformed into the expressionorganism.

The DNA sequence to be mutagenized may be conveniently present in agenomic or cDNA library prepared from an organism expressing the parentmaltogenic alpha-amylase. Alternatively, the DNA sequence may be presenton a suitable vector such as a plasmid or a bacteriophage, which as suchmay be incubated with or otherwise exposed to the mutagenising agent.The DNA to be mutagenized may also be present in a host cell either bybeing integrated in the genome of said cell or by being present on avector harbored in the cell. Finally, the DNA to be mutagenized may bein isolated form. It will be understood that the DNA sequence to besubjected to random mutagenesis is preferably a cDNA or a genomic DNAsequence.

In some cases it may be convenient to amplify the mutated DNA sequenceprior to performing the expression step b) or the screening step c).Such amplification may be performed in accordance with methods known inthe art, the presently preferred method being PCR-generatedamplification using oligonucleotide primers prepared on the basis of theDNA or amino acid sequence of the parent enzyme.

Subsequent to the incubation with or exposure to the mutagenising agent,the mutated DNA is expressed by culturing a suitable host cell carryingthe DNA sequence under conditions allowing expression to take place. Thehost cell used for this purpose may be one which has been transformedwith the mutated DNA sequence, optionally present on a vector, or onewhich was carried the DNA sequence encoding the parent enzyme during themutagenesis treatment. Examples of suitable host cells are thefollowing: gram positive bacteria such as Bacillus subtilis, Bacilluslicheniformis, Bacillus lentus, Bacillus brevis, Bacillusstearothermophilus, Bacillus alkalophilus, Bacillus amyloliquefaciens,Bacillus coagulans, Bacillus circulans, Bacillus lautus, Bacillusmegaterium, Bacillus thuringiensis, Streptomyces lividans orStreptomyces murinus; and gram negative bacteria such as E. coli.

The mutated DNA sequence may further comprise a DNA sequence encodingfunctions permitting expression of the mutated DNA sequence.

Localized Random Mutagenesis

The random mutagenesis may be advantageously localized to a part of theparent maltogenic alpha-amylase in question. This may, e.g., beadvantageous when certain regions of the enzyme have been identified tobe of particular importance for a given property of the enzyme, and whenmodified are expected to result in a variant having improved properties.Such regions may normally be identified when the tertiary structure ofthe parent enzyme has been elucidated and related to the function of theenzyme.

The localized, or region-specific, random mutagenesis is convenientlyperformed by use of PCR generated mutagenesis techniques as describedabove or any other suitable technique known in the art. Alternatively,the DNA sequence encoding the part of the DNA sequence to be modifiedmay be isolated, e.g., by insertion into a suitable vector, and saidpart may be subsequently subjected to mutagenesis by use of any of themutagenesis methods discussed above.

For region-specific random mutagenesis with a view to improving thestability of calcium binding of a parent maltogenic alpha-amylase, codonpositions corresponding to the following amino acid residues from theamino acid sequence set forth in SEQ ID NO: 2 may appropriately betargeted:

Residues:Regions:

16-33, 35-36, 40: 16-40

46-54, 56: 46-56

73-81: 73-81

87-89, 91, 93-96, 99-105, 109: 87-109

129-134, (145, 150): 129-134

167-172, 174, 177, 180-189: 167-189

196-202, 206-210: 196-210

228-235, 237: 228-237

378

637

With a view to achieving improved binding of a substrate, i.e., improvedbinding of a carbohydrate species, such as amylose or amylopectin, by amaltogenic alpha-amylase variant with a modified, e.g. higher, substratespecificity and/or a modified, e.g. higher, specificity with respect tocleavage, i.e. hydrolysis, of the substrate, it appears that thefollowing codon positions in the following regions of the amino acidsequence shown in SEQ ID NO: 2, may particularly appropriately betargeted for modification by region-specific mutagenesis:

70-97, 127-143, 174-198, 226-233, 255-270, 282-292, 324-331, 370-376.

For region-specific random mutagenesis with a view to altering thesubstrate specificity and/or the pH dependent activity profile, thefollowing regions of SEQ ID NO: 2 may be targeted: 70-97, 174-198.

For random mutagenesis with a view to improving the thermostability, theresidues and regions described above may be targeted, particularly thosedescribed for altering stability, filling internal holes, improved Cabinding, interdomain and intradomain contacts, helix capping, prolinesubstitution, and histidine substitution. In addition, the followingregions may be targeted with a view to improving the thermostability:70-109, 167-200. Also, any amino acid residue which is substituted in avariant having improved thermostability may be targeted, e.g. those inthe following positions: 115, 342, 387, 422, 425, 483, 520, 594 and 600.

General Method for Random Mutagenesis by Use of the Dope Program

The random mutagenesis may be carried out by the following steps:

1. Select regions of interest for modification in the parent enzyme

2. Decide on mutation sites and non-mutated sites in the selected region

3. Decide on which kind of mutations should be carried out, e.g. withrespect to the desired stability and/or performance of the variant to beconstructed

4. Select structurally reasonable mutations

5. Adjust the residues selected by step 3 with regard to step 4.

6. Analyse by use of a suitable dope algorithm the nucleotidedistribution.

7. If necessary, adjust the wanted residues to genetic code realism,e.g. taking into account constraints resulting from the genetic code,e.g. in order to avoid introduction of stop codons; the skilled personwill be aware that some codon combinations cannot be used in practiceand will need to be adapted

8. Make primers

9. Perform random mutagenesis by use of the primers

10. Select resulting α-amylase variants by screening for the desiredimproved properties.

Suitable dope algorithms for use in step 6 are well known in the art.One such algorithm is described by Tomandl, D. et al., 1997, Journal ofComputer-Aided Molecular Design 11:29-38. Another algorithm is DOPE(Jensen, L J, Andersen, K V, Svendsen, A, and Kretzschmar, T (1998)Nucleic Acids Research 26:697-702).

Expression of Maltogenic Alpha-Amylase Variants

The construction of the variant of interest is accomplished bycultivating a microorganism comprising a DNA sequence encoding thevariant under conditions which are conducive for producing the variant,and optionally subsequently recovering the variant from the resultingculture broth. This is described in detail further below.

According to the invention, a DNA sequence encoding the variant producedby methods described above, or by any alternative methods known in theart, can be expressed, in the form of a protein or polypeptide, using anexpression vector which typically includes control sequences encoding apromoter, operator, ribosome binding site, translation initiationsignal, and, optionally, a repressor gene or various activator genes.

The recombinant expression vector carrying the DNA sequence encoding anmaltogenic alpha-amylase variant of the invention may be any vectorwhich may conveniently be subjected to recombinant DNA procedures, andthe choice of vector will often depend on the host cell into which it isto be introduced. Thus, the vector may be an autonomously replicatingvector, i.e. a vector which exists as an extrachromosomal entity, thereplication of which is independent of chromosomal replication, e.g. aplasmid, a bacteriophage or an extrachromosomal element, minichromosomeor an artificial chromosome. Alternatively, the vector may be one which,when introduced into a host cell, is integrated into the host cellgenome and replicated together with the chromosome(s) into which it hasbeen integrated.

In the vector, the DNA sequence should be operably connected to asuitable promoter sequence. The promoter may be any DNA sequence whichshows transcriptional activity in the host cell of choice and may bederived from genes encoding proteins either homologous or heterologousto the host cell. Examples of suitable promoters for directing thetranscription of the DNA sequence encoding a maltogenic alpha-amylasevariant of the invention, especially in a bacterial host, are thepromoter of the lac operon of E. coli, the Streptomyces coelicoloragarase gene dagA promoters, the promoters of the Bacillus licheniformisα-amylase gene (amyL), the promoters of the Bacillus stearothermophilusmaltogenic amylase gene (amyM), the promoters of the Bacillusamyloliquefaciens α-amylase (amyQ), the promoters of the Bacillussubtilis xylA and xylB genes, etc. For transcription in a fungal host,examples of useful promoters are those derived from the gene encoding A.oryzae TAKA amylase, Rhizomucor miehei aspartic proteinase, A. nigerneutral α-amylase, A. niger acid stable α-amylase, A. nigerglucoamylase, Rhizomucor miehei lipase, A. oryzae alkaline protease, A.oryzae triose phosphate isomerase or A. nidulans acetamidase.

The expression vector of the invention may also comprise a suitabletranscription terminator and, in eukaryotes, polyadenylation sequencesoperably connected to the DNA sequence encoding the maltogenicalpha-amylase variant of the invention. Termination and polyadenylationsequences may suitably be derived from the same sources as the promoter.

The vector may further comprise a DNA sequence enabling the vector toreplicate in the host cell in question. Examples of such sequences arethe origins of replication of plasmids pUC19, pACYC177, pUB110, pE194,pAMB1 and pIJ702.

The vector may also comprise a selectable marker, e.g. a gene theproduct of which complements a defect in the host cell, such as the dalgenes from B. subtilis or B. licheniformis, or one which confersantibiotic resistance such as ampicillin, kanamycin, chloramphenicol ortetracycline resistance. Furthermore, the vector may compriseAspergillus selection markers such as amdS, argB, niaD and sC, a markergiving rise to hygromycin resistance, or the selection may beaccomplished by co-transformation, e.g. as described in WO 91/17243.

While intracellular expression may be advantageous in some respects,e.g. when using certain bacteria as host cells, it is generallypreferred that the expression is extracellular. In general, the Bacillusα-amylases mentioned herein comprise a preregion permitting secretion ofthe expressed protease into the culture medium. If desirable, thispreregion may be replaced by a different preregion or signal sequence,conveniently accomplished by substitution of the DNA sequences encodingthe respective preregions.

The procedures used to ligate the DNA construct of the inventionencoding maltogenic alpha-amylase variant, the promoter, terminator andother elements, respectively, and to insert them into suitable vectorscontaining the information necessary for replication, are well known topersons skilled in the art (cf., for instance, Sambrook et al. (1989)).

The cell of the invention, either comprising a DNA construct or anexpression vector of the invention as defined above, is advantageouslyused as a host cell in the recombinant production of a maltogenicalpha-amylase variant of the invention. The cell may be transformed withthe DNA construct of the invention encoding the variant, conveniently byintegrating the DNA construct (in one or more copies) in the hostchromosome. This integration is generally considered to be an advantageas the DNA sequence is more likely to be stably maintained in the cell.Integration of the DNA constructs into the host chromosome may beperformed according to conventional methods, e.g. by homologous orheterologous recombination. Alternatively, the cell may be transformedwith an expression vector as described above in connection with thedifferent types of host cells.

The cell of the invention may be a cell of a higher organism such as amammal or an insect, but is preferably a microbial cell, e.g. abacterial or a fungal (including yeast) cell.

Examples of suitable bacteria are gram positive bacteria such asBacillus subtilis, Bacillus licheniformis, Bacillus lentus, Bacillusbrevis, Bacillus stearothermophilus, Bacillus alkalophilus, Bacillusamyloliquefaciens, Bacillus coagulans, Bacillus circulans, Bacilluslautus, Bacillus megaterium, Bacillus thuringiensis, or Streptomyceslividans or Streptomyces murinus, or gram negative bacteria such as E.coli. The transformation of the bacteria may, for instance, be effectedby protoplast transformation or by using competent cells in a mannerknown per se.

The yeast organism may favourably be selected from a species ofSaccharomyces or Schizosaccharomyces, e.g. Saccharomyces cerevisiae. Thefilamentous fungus may advantageously belong to a species ofAspergillus, e.g. Aspergillus oryzae or Aspergillus niger. Fungal cellsmay be transformed by a process involving protoplast formation andtransformation of the protoplasts followed by regeneration of the cellwall in a manner known per se. A suitable procedure for transformationof Aspergillus host cells is described in EP 238 023.

In a yet further aspect, the present invention relates to a method ofproducing a maltogenic alpha-amylase variant of the invention, whichmethod comprises cultivating a host cell as described above underconditions conducive to the production of the variant and recovering thevariant from the cells and/or culture medium.

The medium used to cultivate the cells may be any conventional mediumsuitable for growing the host cell in question and obtaining expressionof the maltogenic alpha-amylase variant of the invention. Suitable mediaare available from commercial suppliers or may be prepared according topublished recipes (e.g. as described in catalogues of the American TypeCulture Collection).

The maltogenic alpha-amylase variant secreted from the host cells mayconveniently be recovered from the culture medium by well-knownprocedures, including separating the cells from the medium bycentrifugation or filtration, and precipitating proteinaceous componentsof the medium by means of a salt such as ammonium sulfate, followed bythe use of chromatographic procedures such as ion exchangechromatography, affinity chromatography, or the like.

Testing of Maltogenic Alpha-Amylase Variants

Maltogenic alpha-amylase variants produced by any of the methodsdescribed above may be tested, either prior to or after purification,for amylolytic activity in a screening assay which measures the abilityof the variant to degrade starch. The screening in step 10 in theabove-mentioned random mutagenesis method of the invention may beconveniently performed by use of a filter assay based on the followingprocedure: A microorganism capable of expressing the mutated maltogenicalpha-amylase of interest is incubated on a suitable medium and undersuitable conditions for secretion of the enzyme, the medium beingcovered with two filters comprising a protein-binding filter placedunder a second filter exhibiting a low protein binding capability. Themicroorganism is grown on the second, top filter. Subsequent to theincubation, the bottom protein-binding filter comprising enzymessecreted from the microorganism is separated from the second filtercomprising the microorganism. The protein-binding filter is thensubjected to screening for the desired enzymatic activity, and thecorresponding microbial colonies present on the second filter areidentified. The first filter used for binding the enzymatic activity maybe any protein-binding filter, e.g., nylon or nitrocellulose. The secondfilter carrying the colonies of the expression organism may be anyfilter that has no or low affinity for binding proteins, e.g., celluloseacetate or Durapore™.

Screening consists of treating the first filter to which the secretedprotein is bound with a substrate that allows detection of the α-amylaseactivity. The enzymatic activity may be detected by a dye, fluorescence,precipitation, pH indicator, IR-absorbance or any other known techniquefor detection of enzymatic activity. The detecting compound may beimmobilized by any immobilizing agent e.g. agarose, agar, gelatine,polyacrylamide, starch, filter paper, cloth; or any combination ofimmobilizing agents. For example, α-amylase activity can be detected byCibacron Red labelled amylopectin, which is immobilized in agarose.α-amylase activity on this substrate produces zones on the plate withreduced red color intensity.

To screen for variants with increased stability, the filter with boundmaltogenic alpha-amylase variants can be pretreated prior to thedetection step described above to inactivate variants that do not haveimproved stability relative to the parent maltogenic alpha-amylase. Thisinactivation step may consist of, but is not limited to, incubation atelevated temperatures in the presence of a buffered solution at any pHfrom pH 2 to 12, and/or in a buffer containing another compound known orthought to contribute to altered stability e.g., surfactants, EDTA,EGTA, wheat flour components, or any other relevant additives. Filtersso treated for a specified time are then rinsed briefly in deionizedwater and placed on plates for activity detection as described above.The conditions are chosen such that stabilized variants show increasedenzymatic activity relative to the parent after incubation on thedetection media.

To screen for variants with altered thermostability, filters with boundvariants are incubated in buffer at a given pH (e.g., in the range frompH 2-12) at an elevated temperature (e.g., in the range from 50°-110°C.) for a time period (e.g., from 1-20 minutes) to inactivate nearly allof the parent maltogenic alpha-amylase, rinsed in water, then placeddirectly on a detection plate containing immobilized Cibacron Redlabelled amylopectin and incubated until activity is detectable.Similarly, pH dependent stability can be screened for by adjusting thepH of the buffer in the above inactivation step such that the parentmaltogenic alpha-amylase is inactivated, thereby allowing detection ofonly those variants with increased stability at the pH in question. Toscreen for variants with increased calcium-dependent stability calciumchelators, such as ethylene glycol-bis(β-aminoethyl ether)N,N,N′,N′-tetraacetic acid (EGTA), is added to the inactivation bufferat a concentration such that the parent maltogenic alpha-amylase isinactivated under conditions further defined, such as buffer pH,temperature or a specified length of incubation.

The variants of the invention may be suitably tested by assaying thestarch-degrading activity of the variant, for instance by growing hostcells transformed with a DNA sequence encoding a variant on astarch-containing agarose plate and identifying starch-degrading hostcells as described above. Further testing in regard to alteredproperties, including specific activity, substrate specificity, cleavagepattern, thermoactivation, thermostability, pH dependent activity oroptimum, pH dependent stability, temperature dependent activity oroptimum, transglycosylation activity, stability, and any other parameterof interest, may be performed on purified variants in accordance withmethods known in the art as described below.

Degradation of β-Limit Dextrin by Maltogenic Alpha-Amylase:

Another important parameter in the evaluation of the substratespecificity of maltogenic alpha-amylase variants may be the degree towhich such enzymes are capable of degrading starch that has beenexhaustively treated with the exoglycosylase β-amylase. To screen forvariants which show patterns of degradation on such a substratediffering from the patterns produced by the parent maltogenicalpha-amylase the following assay is performed: β-limit dextrin isprepared by incubating 25 ml 1% amylopectin in Mcllvane buffer (48.5 mMcitrate and 193 mM sodium phosphate pH 5.0) with 24 μg/ml β-amylaseovernight at 30° C. Unhydrolysed amylopectin (i.e., β-limit dextrin) isprecipitated with 1 volume 98% ethanol, washed and redissolved in water.1 ml β-limit dextrin is incubated with 18 μl enzymes (at 2.2 mg/ml) and100 μl 0.2 M citrate-phosphate pH 5.0 for 2 hrs at 30° C. and analysedby HPLC as described above. Total hydrolysis of β-limit dextrin iscarried out in 2M HCl at 95° C. The concentration of reducing ends ismeasured by methods known in the art.

Calcium Binding Affinity

Unfolding of maltogenic alpha-amylases by exposure to heat or todenaturants such as guanidine hydrochloride is accompanied by a decreasein fluorescence, and oss of calcium ions leads to unfolding. Thus, theaffinity of a maltogenic alpha-amylase variant for calcium can bemeasured by fluorescence measurements before and after incubation of thevariant (e.g., at a concentration of 10 mg/ml) in a buffer (e.g., 50 mMHEPES, pH 7) with different concentrations of calcium (e.g., in therange from 1 mM-100 mM) or of EGTA (e.g., in the range from 1-1000 mM)for a sufficiently long period of time (such as 22 hours at 55° C.).

The measured fluorescence, F, is composed of contributions form thefolded and unfolded forms of the enzyme. The following equation can bederived to describe the dependence of F on calcium concentration ([Ca]):

F=[Ca]/(K _(diss)[Ca])(a _(N) −b _(N) log([Ca]))+K _(diss)/(K_(diss)[Ca])(a _(U) −b _(U) log([Ca]))

where a_(N) is the fluorescence of the native (folded) form of theenzyme, b_(N) is the linear dependence of a_(N) on the logarithm of thecalcium concentration (as observed experimentally), a_(U) is thefluorescence of the unfolded form and b_(U) is the linear dependence ofa_(U) on the logarithm of the calcium concentration. K_(diss) is theapparent calcium binding constant for an equilibrium process as follows:

K_(diss)

N—Ca<<U+Ca(N=native enzyme; U=unfolded enzyme)

In fact, unfolding proceeds extremely slowly and is irreversible. Therate of unfolding is dependent on calcium concentration, and suchdependency for a given enzyme provides a measure of the calcium bindingaffinity of the enzyme. By defining a standard set of reactionconditions (e.g., 22 hours at 55° C.), a meaningful comparison ofK_(diss) for different maltogenic alpha-amylase variants can be made.

INDUSTRIAL APPLICATIONS

The maltogenic alpha-amylase variants of the invention possess valuableproperties which may be advantageously used in various industrialapplications. In particular, the enzyme finds potential application forretarding or preventing retrogradation, and thus the staling, of starchbased food such as common in the baking industry.

The variant may be used for the preparation of bread and other breadproducts in accordance with conventional techniques known in the art.

It is believed that the modification of the starch fraction by use ofthe present invention results in increased volume in baked products andimproved organoleptic qualities, such as flavour, mouth feel,palatability, aroma and crust colour.

The maltogenic alpha-amylase variant may be used as the only enzyme oras a major enzymatic activity in combination with one or more additionalenzymes, such as xylanase, lipase, glucose oxidase and otheroxidoreductases, or an amylolytic enzyme.

The enzyme variants of the invention also find industrial applicabilityas a component in washing, dishwashing and hard-surface cleaningdetergent compositions. Some variants are particularly useful in aprocess for the manufacture of linear oligosaccharides, or in theproduction of sweeteners and ethanol from starch, and/or for textiledesizing. Conditions for conventional starch conversion processes,including starch liquefaction and/or saccharification processes, aredescribed in, e.g., U.S. Pat. No. 3,912,590 and in EP patentpublications Nos. 252,730 and 63,909.

The invention is further illustrated with reference to the followingexamples which are not intended to be in any way limiting to the scopeof the invention as claimed.

Determination of Maltogenic Amylase in MANU

One Maltogenic Amylase Novo Unit (MANU) is the amount of enzyme whichunder standard will cleave one μmol maltotriose per minute. The standardconditions are 10 mg/ml maltotriose, 37° C., pH 5.0, 30 minutes reactiontime.

The pH dependence is found by repeating this measurement at the sameconditions, but at different pH values.

EXAMPLES Example 1 Construction of a variant of Novamyl with altered pHdependent activity

Novamyl is expressed in Bacillus subtilis from a plasmid denoted hereinas pLBei010. This plasmid contains amyM in which the expression of amyMis directed by its own promoter and the complete gene encoding Novamyl,e.g., as contained in the strain DSM 11837. The plasmid contains theorigin of replication, al, from plasmid pUB110 and an kanamycinresistance marker for selection purposes. pLBei010 is shown in FIG. 1.

Primer Sequences

Site directed mutants of Novamyl were constructed by the megaprimermethod essentially as described by Kammann et al. (1989). Briefly, amutagenic oligonucleotide primer is used together in a PCR reaction witha suitable opposite DNA strand end primer to create a preliminary PCRproduct. This product is then used as a megaprimer together with anotheropposite DNA strand end primer to create a double-stranded DNA product.The product of the final PCR reaction was routinely used to replace acorresponding DNA fragment in the pLBei010 plasmid by standard cloningprocedures. Mutants were transformed directly into Bacillus subtilisstrain SHa273, a derivative of Bacillus subtilis 168 which is apr⁻,npr⁻, amyE⁻, amyR2⁻ and prepared by methods known in the art.

Oligonucleotide primers used in the construction of described variantsare as listed below:

Variant Sequence (5′→3′)

F188H: SEQ ID NO: 3

F188E: SEQ ID NO: 4

F284E: SEQ ID NO: 5

F284D: SEQ ID NO: 6

F284K: SEQ ID NO: 7

N327D: SEQ ID NO: 8

Variant Sequence (3′→5′)

T288K: SEQ ID NO: 9

T288R: SEQ ID NO: 10

Aspartate variants of F284, T288 and N327 were obtained using primerA189 (SEQ ID NO: 11) and B649 (SEQ ID NO: 12) as end-primers.

F188-variants F188L, T189Y were obtained using primer A82 (SEQ ID NO:13) and B346 (SEQ ID NO: 14) as end-primers.

PCR products with the desired modification(s) were purified, digestedwith appropriate enzymes, separated by agarose gel electrophoresis andextracted, ethanol precipitated in the presence of glycogen, resuspendedin H₂O, ligated to pLBei010 which had been digested with the sameappropriate enzymes, and transformed into Bacillus subtilis SHa273.Transformants were checked for size by colony PCR and for the insertionor removal of specific restriction sites by restriction enzymedigestion. Positive colonies were verified by DNA sequencing methods asdescribed in the art.

Fermentation

The B. subtilis SHa273 mutant clones were grown overnight on LB-Kana (10μg/ml)-Starch plates at 37° C. The colonies from the plate wereresuspended in 10 ml Luria broth. One-sixth of each of the suspensionswere inoculated into a 500 ml shake flasks containing 100 ml PS-1 media,a soy meal/sucrose-based media, kanamycin for a final concentration of10 μg/ml and 100 μl 5M NaOH. The pH was adjusted to 7.5 with NaOH beforeinoculation. The cultures were incubated for five days at 30° C. withshaking at 270-300 rpm.

Enzyme Purification

Large particles from the media were removed by flocculation beforeaffinity chromatography. Superfloc C521 (American Cyamide Company) wasused as the cationic flocculant and Superfloc A130 (American CyamideCompany) as the anionic flocculant.

The culture suspension was diluted 1:1 with deionized water and the pHwas adjusted to approx. 7.5. A volume of 0.01 ml of 50w/w % CaCl₂ per mldiluted culture was added during stirring. A volume of 0.015 ml of 20w/w% Na-aluminate per ml diluted culture was titrated with 20% formic acid,while keeping the pH between 7 and 8. While stirring 0.025 ml 10v/v % ofC521 per ml diluted culture was added, followed by 0.05 ml 1w/v % A130per ml diluted culture, or until flocculation was observed. The solutionwas centrifuged at 4500 rpm for 30 minutes. Filtration was performedusing a filter of pore size of 0.45 μm to exclude larger particles andany remaining bacteria. The filtered solution was stored at −20° C.

Immobilization of α-cyclodextrin to DSV-agarose

One hundred mg of α-cylcodextrin of molecular weight 972.86 g/mol (Fluka28705) was dissolved in 20 ml coupling buffer (0.5M Na₂CO₃, pH 11). Tenml of DSV-agarose (Mini-Leak, Medium 10-20 mmol/l of divinyl sulfoneactivated agarose (Kem-En-Tec) was washed thoroughly with deionizedwater, then dried by suction and transferred to the a-cyclodextrinsolution. After the mixture had stirred for 24 hr at ambienttemperature, the gel was washed with deionized water, followed by 0.5MKHCO₃. The gel was transferred to the blocking buffer (20 ml 0.5MKHCO₃+1 ml mercaptoethanol), stirred for 2 hr at ambient temperature,then washed with deionized water.

Affinity Chromatography

The variants were purified by affinity chromatography using thePharmacia FPLC System. A 0.04 volume of 1M Na-acetate pH 5 was added tothe filtrate obtained by flocculation to adjust pH and CaCl₂ was addedto a final concentration of 10⁻¹⁰ M. The solution was filtered anddegassed. A Pharmacia XK16 column was prepared with ten ml of theimmobilised α-cyclodextrin, then equilibrated in the equilibrationbuffer (25 mM Na-acetate pH 5) by washing with approximately 10 timesthe column volume. The filtrate was applied to the XK16 column, whichwas then washed with the equilibration buffer until protein could nolonger be detected in the washing buffer. The column was washed with theequilibration buffer containing 0.5M NaCl to elute nonspecific material,followed by another wash with 2-3 times the column volume of theequilibration buffer. All washings were performed using a flow rate of10 ml/min. Specifically bound material was eluted using a solution of 2%α-cyclodextrin in the wash buffer and collected using the PharmaciaLiquid Chromatography Collector LCC-500 Plus using a flow rate of 5ml/min.

Example 2 pH Dependent Activity of Variants

The variants prepared in the preceding Example were tested for activityat various pH values as follows.

A colorimetric glucose oxidase-peroxidase assay for liberated glucosefrom maltotriose or amylopectin was used to determine the pH activityprofiles of the enzyme variants (Glucose/GOD-Perid® Method, BoehringerMannheim, Indianapolis Ind.). Activity was assayed in a buffer of 25 mMcitrate-phosphate, 0.1 mM CaCl₂ at pH values of 2, 2.5, 3, 3.5, 4, 4.5,5, 5.5, 6, 6.5, 7, 7.5, 8 and 8.6. The buffer pH was adjusted using NaOHand enzymes were diluted in 25 mM citrate-phosphate buffer pH 5.Measurements were taken in duplicate to obtain an average value. Allvalues are relative to the pH at which the highest level of activity isseen.

The results, shown in the table below, indicate that each of thevariants has an alteration in the pH dependent activity profile whencompared to the parent Novamyl®. The highest level of activity for eachvariant is designated 100% and the activity of that variant measured atthe other indicated pH values is a relative percentage of that maximum.

pH Modifications 2.0 2.5 3.0 3.5 4.0 4.5 5.0 5.5 6.0 6.5 7.0 7.5 8.0 8.6None (parent) 0 0 0 8 47 80 100 95 91 80 66 39 35 30 F188H 1 0 0 1 3 2977 99 100 88 59 39 31 27 F188E 0 0 0 2 27 62 89 100 93 71 46 28 20 18T288R 0 0 0 8 51 77 94 100 86 73 50 34 27 12 N327D 1 1 7 27 67 95 100 9877 33 19 11 5 0

Further, a number of Novamyl variants were tested for activity at pH 4.0and 5.0, taking the activity of Novamyl at the same pH as 100%. Theactivity was determined by hydrolysis of maltotriose (10 mg/ml) at 60°C., 50 mM sodium acetate, 1 mM CaCl₂. The results are expressed as theratio between activity at pH 5.0 and pH 4.0:

Modifications pH 5.0/pH 4.0 N131D 0.24 I174Q 0.31 G397P 0.40 H103Y 0.40Δ 262-266 0.47 T142A + D261G + T288P + Q449R 0.50 S32Q 0.53 S32D 0.55T142A + D261G 0.62 G370N + N371G 0.66 S32N 0.68 N176S 0.79 D17E 0.80None (parent) 1 Δ 191 1.39 192-A-193 1.61 I174E 1.80 192-A-G-193 1.90 Δ192 2.22 F188L + D261G + T288P 2.47

The results demonstrate that variants with a higher or lower pH optimumcan be obtained according to the invention.

Example 3 Thermostability of Variants Incubation at 80° C.

The thermostability of a number of Novamyl variants was tested byincubating an aqueous solution at 80° C., pH 4.3, 50 mM acetate buffer,1 mM CaCl₂, and measuring the residual amylase activity at varioustimes. The parent enzyme, Novamyl, was included for comparison. Theresults are expressed as residual activity at various times in percentof initial activity:

5 10 15 20 25 Variant 0 min. min. min. min. min. None (parent) 100 23 93 1 0 A197P + D261G + T288P + 100 36 28 14 16 9 N342S A30D + K40R +D261G 100 38 24 15 13 10 T288K 100 64 31 18 7 4 T142A + N327S + K425E +100 47 39 25 19 11 K520R + N595I T142A + D261G + T288P + 100 45 36 27 169 Q449R K40R + F188L + D261G + 100 56 48 40 36 30 A483T F188L + V336L +T525A 100 63 49 48 52 47 F188I + Y422F + I660V 100 71 60 51 43 38N115D + F188L 100 73 60 51 44 39 F188L + D261G + T288P 100 60 67 66 6367 F188L + D261G + T288P + 100 66 72 73 75 78 A483T N26S + F188L +D261G + 100 80 80 82 84 84 T288P + T594A + I600V N26S + T80A + F188L +100 80 75 82 83 87 D261G + T288P + R291L

The above data show a clearly improved thermostability for the variantscompared to the parent amylase. Thus, after 15 minutes incubation at 80°C., a number of variants show at least 25% residual activity, and someeven show at least 50% residual activity, whereas the parent enzyme hasessentially lost its activity.

Incubation at 85° C.

The Novamyl variant S32E was tested by incubation with 1 mM Ca⁺⁺ at 85°C. for 15 minutes. The variant showed a residual activity of 48% whereasthe parent enzyme (Novamyl) showed 32% residual activity at the sameconditions.

Incubation at 90° C.

Four variants and the parent enzyme were tested by incubating at 90° C.,pH 5.0, 50 mM acetate buffer, 1 mM CaCl₂, and measuring the residualactivity. The results were as follows:

Variant 0 10 min. 20 min. 30 min. None (parent) 100 5 0 0 F188L +D261G + T288P 100 70 41 28 N26S + F188L + D261G + 100 71 54 39 T288P +T594A + I600V N26S + T80A + F188L + 100 43 26 13 D261G + T288P + R291LF188L + D261G + T288P + A483T 100 54 39 26

The variants show a clearly improved thermostability. Thus, the variantsretain more than 10% (or even more than 20%) relative activity after 30minutes incubation at 90° C., whereas the parent enzyme loses allactivity after 20 minutes.

DSC

Further, the thermostability was tested for some Novamyl variants by DSC(differential scanning calorimetry) at pH values in the range 4.0-5.5.Again, the parent amylase was included for comparison. The results areexpressed as the denaturation temperature (Tm) at the given pH:

Modifications pH 4.0 pH 4.3 pH 5.0 pH 5.5 None (parent) 64° C. 79° C.83° C. 88° C. N115D + F188L 86° C. 92° C. T142A + N327S + K425E + 93° C.K520R + N595I F188L + D261G + T288P 75° C. 95° C.

The results show improved thermostability for each variant. One variantshows an improvement of more than 10° C. at pH 4.0 and 5.5.

Example 4 Specific Activity of Variants

Amylase activity was determined by a colorimetric measurement afteraction on Phadebas tablets at pH 5.0 and 60° C. The results for twoNovamyl variants, relative to Novamyl were as follows:

Modifications Relative amylase activity None (parent) 100 192-A-193 110Δ (191-195) 300

The specific activity was further tested by action on maltotriose at pH4.0, 60° C. by the MANU method described above. The results showed thatthe variant G370N,N371G has a maltotriose activity of 106% compared toNovamyl.

Example 5 Inhibition of Retrogradation

The efficiency of Novamyl and Novamyl variants to inhibit retrogradationwas determined as follows:

730 mg of 50% (w/w) amylopectin slurry in 0.1 M sodium acetate, at aselected pH (3.7, 4.3 or 5.5) was mixed with 20 μl of an enzyme sample,and the mixture was incubated in a sealed ampoule for 1 hour at 40° C.,followed by incubation at 100° C. for 1 hour in order to gelatinize thesamples. The sample was then aged for 7 days at room temperature toallow recrystallization of the amylopectin. A control without enzyme wasincluded.

After aging, DSC was performed on the sample by scanning from 5° C. to95° C. at a constant scan rate of 90° C./hour. The area under the firstendothermic peak in the thermogram was taken to represent the amount ofretrograded amylopectin, and the relative inhibition of retrogradationwas taken as the area reduction (in %) relative to the control withoutenzyme.

In the table below, the efficiency of the enzyme is expressed as theratio of the relative inhibition of retrogradation to the enzyme dosage(in MANU/ml):

Relative pH Modifications MANU/ml inhibition Efficiency 3.7 A30D +K40R + D261G 0.23 0.38 1.7 3.7 T142A + N327S + K425E + 0.07 0.29 4.1K520R + N595I 3.7 None (parent) 0.27 0.38 1.4 4.3 N115D + F188L 0.010.18 18 4.3 None (parent) 0.27 0.43 1.6 5.5 Δ (191-195) + F188L + T189Y0.02 0.12 6 5.5 Δ (191-195) 0.02 0.14 7 5.5 Δ (191-195) 0.05 0.31 6.25.5 N115D + F188L 0.01 0.39 39 5.5 T142A + D261G 0.14 0.53 3.8 5.5 None(parent) 0.27 0.49 1.8

The results demonstrate that a number of variants are more efficientthan the parent amylase to inhibit retrogradation.

Example 6 Anti-Staling Effect of Variants

Bread was made by an European Straight Dough method (wheat flour, water,yeast, salt, sugar, ascorbic acid) or from a wheat sour dough (acidifiedwith “Ireks ferdigsauer” from Balchem Co.) with or without addition ofenzymes, and loaves were baked in lidded pans, to avoid volume effects.pH in the dough was measured by blending 10 g of the mixed dough with100 ml of deionised water for 30 min before measurement of pH in thesuspension. The bread was allowed to cool for 2 hours, and the texturewas analyzed by a Texture Analyser TA-XT2 from Stable Micro Systems. Theremaining loaves were then wrapped in plastic bags and stored at roomtemperature for texture analysis after 1, 4 and 7 days.

The texture analysis of each loaf was done by cutting 4 slices; theforce was measured at 25% compression (P1), at 40% compression (P2) andafter keeping 40% compression constant for 30 sec. (P3). P1 was taken asthe firmness (in grams), and the ratio (P3/P2) was taken as theelasticity of the crumb. The extent of retrogradation after 7 daysstorage was determined by DSC as described in Example 7.

European Straight Dough (pH5.5-6.0)

A Novamyl variant (T142A+N327S+K425E+K520R+N5951) was tested at dosagesin the range of 0-2 mg enzyme/kg flour, and the parent enzyme (Novamyl)was used for comparison.

The following results were obtained for elasticity (P3/P2) after twohours and 7 days and firmness (P1) after 7 days:

Dosage Elasticity Elasticity Elasticity Enzyme mg/kg flour 2 hours 1 day7 days None 0 0.69 0.60 0.44 Parent 1 0.62 0.60 0.55 2 0.58 0.57 0.54Variant 1 0.65 0.62 0.56 2 0.63 0.61 0.58

Dosage Firmness (P1) Enzyme mg/kg flour after 7 days None 0 2267 Parent1 1192 2 1113 Variant 1 1022 2 905

The results after two hours and 1 day show that at equal dosages, thevariant gives a better elasticity than the parent enzyme. The resultsafter 7 days show that the variant at dosages of 1-2 mg/kg gives asofter crumb (lower firmness and higher elasticity) than the parentenzyme at the same dosage. Thus, the variant has a better anti-stalingeffect throughout a 7-day storage period.

Sour Dough (pH Approx. 4.5)

A Novamyl variant (F188L+D261G+T288P) was tested in sour dough, and theparent enzyme (Novamyl) was used for comparison. The following resultswere obtained for firmness (P1) after 7 days, elasticity (P3/P2) after 4and 7 days and retrogradation after 7 days:

Dosage Firmness (P1) Enzyme mg/kg flour after 7 days None 0 2590 Parent1 2031 3 1912 13 1570 Variant 1 1436 3 1226

Dosage Elasticity Elasticity Enzyme mg/kg flour 4 days 7 days None 00.49 0.47 Parent 1 0.51 0.52 3 0.53 0.51 13 0.53 0.51 Variant 1 0.590.57 3 0.57 0.58

Dosage Retrogradation, 7 days Enzyme mg/kg flour (relative to control)None 0 100% Parent 1 100% 3 63% 13 32% Variant 1 46% 3 20%

The results show that the variant has a markedly improved effect ontexture evaluated as firmness and elasticity in sour dough at pH 4.5. Adosage of 1-3 mg/kg of the variant is superior to 13 mg/kg of the parentenzyme on all parameters tested, and the elasticity achieved with thevariant cannot be matched by the parent enzyme at any dosage.

pH-profile in wheat-flour bread (pH Approx. 4.4; 4.9; and 5.5)

The Novamyl variant (F188L+D261G+T288P) was further tested in acidifiedwheat flour bread to measure the function over a broader pH range inbaking application, while maintaining a comparable recipe. The parentenzyme (Novamyl) was used for comparison. Dosage of the parent enzymewas changed at the various pH to compensate for the lower activity ofthe parent enzyme at lower pH. The following results were obtained forfirmness (P1) and elasticity (P3/P2) after 0 (=2 hours), 1, 3 and 7days.

Dosage pH Enzyme mg/kg flour 0 days 1 day 3 days 7 days Firmness pH 4.4None 0 450 1144 1945 3020 Variant 0.5 392 939 1386 1664 Parent 15 8701206 1220 1511 Parent 1 586 1127 2005 2312 pH 4.9 None 0 330 764 15362005 Variant 0.5 287 687 767 1096 Parent 7 570 1075 984 1057 Parent 0.5373 784 1170 1642 pH 5.5 None 0 217 711 1123 1382 Variant 0.5 315 447712 846 Parent 3.5 431 629 666 718 Parent 0.5 381 599 630 922 ElasticitypH 4.4 None 0 0.70 0.61 0.53 0.48 Variant 0.5 0.70 0.63 0.59 0.56 Parent15 0.53 0.50 0.52 0.51 Parent 1 0.65 0.60 0.55 0.51 pH 4.9 None 0 0.710.64 0.55 0.49 Variant 0.5 0.70 0.65 0.63 0.60 Parent 7 0.56 0.52 0.540.54 Parent 0.5 0.67 0.61 0.58 0.54 pH 5.5 None 0 0.70 0.61 0.56 0.51Variant 0.5 0.68 0.64 0.61 0.60 Parent 3.5 0.58 0.56 0.57 0.57 Parent0.5 0.63 0.61 0.62 0.58

It is clearly observed, that the variant is much improved compared tothe parent at all pH, and especially at lower pH. The elasticity ishigher, and the crumb stays more soft over the measured time span.

Four Variants Tested in Wheat Sourdough Compared to Parent Enzyme

Four Novamyl variants were tested in another test series of acidifiedwheat flour bread to determine the performance in sourdough bakingapplication. pH in the bread and dough was measured to be in theinterval 4.30-4.40. The parent enzyme (Novamyl) was used for comparison.Dosage of the parent enzyme was chosen at 1 and 13 mg/kg flour, muchhigher than the variants, as we have experienced that this is needed tosee effect of the parent enzyme in this specific application. Thefirmness (P1) and elasticity (P3/P2) were determined after 1, 3 and 7days, and the extent of retrogradation after 7 days storage wasdetermined as described above.

Dosage Firmness Enzyme mg/kg flour 1 day 3 days 7 days None 0 789 16242054 Parent 1 745 1107 1685 13 722 967 1205 N26S + F188L + D261G + 0.5716 1170 1518 T288P + T594A + I600V 3 847 895 1188 F188L + D261G + T288P0.5 689 1054 1457 A197P + D261G + T288P + 0.5 638 1114 1631 N342SF188L + D261G + T288P + 0.5 643 983 1562 A483T 3 660 804 953

Dosage Elasticity Enzyme mg/kg flour 1 day 3 days 7 days None 0 0.630.55 0.48 Parent 1 0.64 0.57 0.49 13 0.57 0.56 0.53 N26S + F188L +D261G + 0.5 0.63 0.56 0.50 T288P + T594A + I600V 3 0.61 0.59 0.57F188L + D261G + T288P 0.5 0.64 0.58 0.53 A197P + D261G + T288P + 0.50.64 0.57 0.50 N342S F188L + D261G + T288P + 0.5 0.65 0.58 0.53 A483T 30.63 0.60 0.58

Dosage mg/kg Retrogradation, 7 days Enzyme flour (relative to control)None 0 100% Parent 1 67% 13 21% N26S + F188L + D261G + T288P + 0.5 72%T594A + I600V 3 18% F188L + D261G + T288P 0.5 53% A197P + D261G +T288P + N342S 0.5 59% F188L + D261G + T288P + A483T 0.5 43% 3 10%

For antistaling (fresh-keeping) it is particularly important, that thebread is soft and elastic after several days storage. Therefore, mostweight should be put on the textural properties after 7 days of storage.It is clearly observed, that the variants are much improved compared tothe parent. The elasticity is higher, and the crumb stays more soft.

Example 7 Cleavage Pattern of Variants

The cleavage pattern in starch hydrolysis was compared for two variantsand the parent enzyme, Novamyl.

The results below indicate % by weight of each oligosacccharide (G1-G8)formed after 24 hours incubation in 1% (w/v) starch using 50 mM sodiumacetate, 1 mM CaCl₂, pH 5.0 at 50° C. The oligosaccharides wereidentified and quantitated using HPLC.

Oligosaccharide Parent Δ (191-195) N115D + F188L G8 — 1.7 — G7 — 2.6 —G6 — 7.5 1.4 G5 — 10.1 2.1 G4 — 21.1 11.3 G3 — 28.7 10.7 G2 96.5 28.361.9 G1 3.5 — 12.6

The results demonstrate a significantly altered cleavage pattern.Novamyl after 24 hours produces mainly maltose and virtually no higheroligosaccharides. In contrast, the two variants produce significantamounts of maltotriose and higher oligosaccharides.

Example 8 Substrate Specificity of Variants

The activity of variants was tested on two different substrates: glucoserelease from maltotriose and color release from Phadebas colored starch.The parent enzyme (Novamyl) was tested for comparison. The measurementswere made at pH 5, and each activity was expressed relative to theparent enzyme. The ratio of activities on the two substrates was foundto be as follows:

Activity ratio Variant Starch/maltotriose Parent enzyme 1.0 F188L,D261G, T288P 3.6 N26S + F188L, D261G, T288P, T594A, I600V 5.5 N26S,T80A, F188L, D261G, T288P, R291L 1.9 A197P, D261G, T288P, N342S 1.5T142A, D261G, T288P, Q449R 2.5 F188L, D261G, T288P, A483T 2.5

It is seen that the 6 variants have an increased activity on starchrelative to maltotriose.

REFERENCES CITED

-   Klein, C., et al., Biochemistry 1992, 31, 8740-8746,-   Mizuno, H., et al., J. Mol. Biol. (1993) 234, 1282-1283,-   Chang, C., et al, J. Mol. Biol. (1993) 229, 235-238,-   Larson, S. B., J. Mol. Biol. (1994) 235, 1560-1584,-   Lawson, C. L., J. Mol. Biol. (1994) 236, 590-600,-   Qian, M., et al., J. Mol. Biol. (1993) 231, 785-799,-   Brady, R. L., et al., Acta Crystallogr. sect. B, 47, 527-535,-   Swift, H. J., et al., Acta Crystallogr. sect. B, 47, 535-544-   A. Kadziola, Ph.D. Thesis: “An alpha-amylase from Barley and its    Complex with a Substrate Analogue Inhibitor Studied by X-ray    Crystallography”, Department of Chemistry University of Copenhagen    1993-   MacGregor, E. A., Food Hydrocolloids, 1987, Vol. 1, No. 5-6, p.-   B. Diderichsen and L. Christiansen, Cloning of a maltogenic    α-amylase from Bacillus stearothermophilus, FEMS Microbiol. letters:    56: pp. 53-60 (1988)-   Hudson et al., Practical Immunology, Third edition (1989), Blackwell    Scientific Publications, Sambrook et al., Molecular Cloning: A    Laboratory Manual, 2nd Ed., Cold Spring Harbor, 1989-   S. L. Beaucage and M. H. Caruthers, Tetrahedron Letters 22, 1981,    pp. 1859-1869-   Matthes et al., The EMBO J. 3, 1984, pp. 801-805.-   R. K. Saiki et al., Science 239, 1988, pp. 487-491.-   Morinaga et al., (1984, Biotechnology 2:646-639)-   Nelson and Long, Analytical Biochemistry 180, 1989, pp. 147-151-   Hunkapiller et al., 1984, Nature 310:105-111-   R. Higuchi, B. Krummel, and R. K. Saiki (1988). A general method of    in vitro preparation and specific mutagenesis of DNA fragments:    study of protein and DNA interactions. Nucl. Acids Res.    16:7351-7367.-   Dubnau et al., 1971, J. Mol. Biol. 56, pp. 209-221.-   Gryczan et al., 1978, J. Bacteriol. 134, pp. 318-329.-   S. D. Erlich, 1977, Proc. Natl. Acad. Sci. 74, pp. 1680-1682.-   Boel et al., 1990, Biochemistry 29, pp. 6244-6249.-   Kammann, M Laufs, J Schell, J and Gronnenborn, B (1989) Nucleic    Acids Research 20:4937-4938.

TABLE 1 Atom Coordinates from the Crystal Structure of NOVAMYL 1 N SER A1 10.254 56.595 38.175 1.00 15.64 7 2 CA SER A 1 11.216 55.462 37.8981.00 15.87 6 3 C SER A 1 12.466 55.723 38.726 1.00 14.53 6 4 O SER A 112.585 56.773 39.369 1.00 15.99 8 5 CB SER A 1 11.527 55.345 36.397 1.0021.54 6 6 OG SER A 1 12.305 56.503 36.045 1.00 20.33 8 7 N SER A 213.466 54.795 38.551 1.00 18.07 7 8 CA SER A 2 14.705 55.061 39.291 1.0019.33 6 9 C SER A 2 15.621 56.069 38.559 1.00 15.87 6 10 O SER A 216.573 56.563 39.209 1.00 16.73 8 11 CB SER A 2 15.490 53.735 39.4221.00 26.53 6 12 OG SER A 2 15.918 53.392 38.123 1.00 21.07 8 13 N SER A3 15.136 56.545 37.384 1.00 12.71 7 14 CA SER A 3 15.956 57.522 36.6801.00 13.38 6 15 C SER A 3 15.873 58.916 37.316 1.00 12.57 6 16 O SER A 316.759 59.749 37.029 1.00 15.22 8 17 CB SER A 3 15.434 57.682 35.2191.00 16.30 6 18 OG SER A 3 15.593 56.381 34.568 1.00 23.61 8 19 N ALA A4 14.811 59.222 38.050 1.00 10.88 7 20 CA ALA A 4 14.574 60.623 38.3841.00 11.38 6 21 C ALA A 4 15.599 61.115 39.409 1.00 12.81 6 22 O ALA A 415.888 62.314 39.355 1.00 12.58 8 23 CB ALA A 4 13.132 60.682 38.9561.00 14.28 6 24 N SER A 5 15.968 60.306 40.380 1.00 13.21 7 25 CA SER A5 16.905 60.780 41.427 1.00 14.29 6 26 C SER A 5 18.163 59.941 41.3571.00 16.01 6 27 O SER A 5 18.053 58.724 41.237 1.00 16.41 8 28 CB SER A5 16.218 60.613 42.785 1.00 15.57 6 29 OG SER A 5 17.193 60.855 43.8431.00 13.17 8 30 N VAL A 6 19.340 60.530 41.476 1.00 10.07 7 31 CA VAL A6 20.589 59.751 41.567 1.00 10.13 6 32 C VAL A 6 21.169 59.955 42.9631.00 10.99 6 33 O VAL A 6 22.349 59.685 43.172 1.00 10.81 8 34 CB VAL A6 21.639 60.160 40.513 1.00 13.85 6 35 CG1 VAL A 6 21.002 59.694 39.1481.00 15.29 6 36 CG2 VAL A 6 21.874 61.656 40.459 1.00 12.12 6 37 N LYS A7 20.369 60.349 43.964 1.00 10.30 7 38 CA LYS A 7 20.901 60.604 45.3311.00 9.78 6 39 C LYS A 7 21.508 59.360 46.015 1.00 12.06 6 40 O LYS A 722.382 59.560 46.857 1.00 12.59 8 41 CB LYS A 7 19.830 61.187 46.2641.00 11.40 6 42 CG LYS A 7 19.414 62.588 45.680 1.00 12.09 6 43 CD LYS A7 18.160 63.123 46.350 1.00 9.80 6 44 CE LYS A 7 17.698 64.488 45.7951.00 10.87 6 45 NZ LYS A 7 17.114 64.187 44.425 1.00 11.38 7 46 N GLY A8 21.036 58.214 45.577 1.00 13.10 7 47 CA GLY A 8 21.604 56.982 46.1661.00 12.31 6 48 C GLY A 8 22.718 56.358 45.340 1.00 14.02 6 49 O GLY A 823.109 55.205 45.579 1.00 13.36 8 50 N ASP A 9 23.133 57.048 44.293 1.0011.90 7 51 CA ASP A 9 24.049 56.447 43.319 1.00 11.74 6 52 C ASP A 925.478 56.996 43.442 1.00 10.18 6 106 CB ILE A 15 37.192 59.653 28.3431.00 10.73 6 107 CG1 ILE A 15 37.106 60.975 29.131 1.00 11.86 6 108 CG2ILE A 15 37.626 60.014 26.904 1.00 12.56 6 109 CD1 ILE A 15 36.18162.091 28.574 1.00 15.42 6 110 N ILE A 16 34.926 57.450 26.561 1.0010.37 7 111 CA ILE A 16 34.728 56.178 25.868 1.00 11.03 6 112 C ILE A 1635.990 55.729 25.099 1.00 12.23 6 113 O ILE A 16 36.342 54.511 25.1841.00 11.07 8 114 CB ILE A 16 33.578 56.292 24.863 1.00 10.56 6 115 CG1ILE A 16 32.240 56.387 25.709 1.00 11.92 6 116 CG2 ILE A 16 33.44455.053 23.953 1.00 11.18 6 117 CD1 ILE A 16 31.115 56.958 24.823 1.0013.67 6 118 N ASP A 17 36.565 56.624 24.314 1.00 10.08 7 119 CA ASP A 1737.730 56.165 23.518 1.00 8.61 6 120 C ASP A 17 38.911 55.693 24.3461.00 10.86 6 121 O ASP A 17 39.777 54.987 23.831 1.00 11.03 8 122 CB ASPA 17 38.184 57.422 22.675 1.00 11.30 6 123 CG ASP A 17 39.380 57.01721.755 1.00 9.77 6 124 OD1 ASP A 17 39.105 56.206 20.852 1.00 11.65 8125 OD2 ASP A 17 40.480 57.562 21.970 1.00 11.48 8 126 N ARG A 18 38.97255.999 25.646 1.00 9.54 7 127 CA ARG A 18 40.113 55.719 26.527 1.00 8.386 128 C ARG A 18 39.826 54.720 27.608 1.00 9.97 6 129 O ARG A 18 40.64354.490 28.501 1.00 13.32 8 130 CB ARG A 18 40.537 57.083 27.137 1.0011.02 6 131 CG ARG A 18 40.931 58.139 26.063 1.00 9.63 6 132 CD ARG A 1842.135 57.721 25.237 1.00 9.86 6 133 NE ARG A 18 42.280 58.523 23.9691.00 10.16 7 134 CZ ARG A 18 43.103 59.578 23.903 1.00 13.46 6 135 NH1ARG A 18 43.748 60.063 24.966 1.00 12.03 7 136 NH2 ARG A 18 43.35060.181 22.725 1.00 10.43 7 137 N PHE A 19 38.648 54.007 27.497 1.0011.25 7 138 CA PHE A 19 38.296 53.057 28.601 1.00 10.13 6 139 C PHE A 1938.543 51.614 28.192 1.00 12.61 6 140 O PHE A 19 39.528 51.024 28.6771.00 12.51 8 141 CB PHE A 19 36.798 53.294 28.945 1.00 13.20 6 142 CGPHE A 19 36.342 52.543 30.189 1.00 12.09 6 143 CD1 PHE A 19 36.84952.908 31.423 1.00 12.96 6 144 CD2 PHE A 19 35.472 51.447 30.058 1.0013.30 6 145 CE1 PHE A 19 36.500 52.187 32.563 1.00 16.46 6 146 CE2 PHE A19 35.184 50.719 31.215 1.00 12.02 6 147 CZ PHE A 19 35.638 51.08932.482 1.00 11.98 6 148 N TYR A 20 37.844 51.054 27.199 1.00 11.48 7 149CA TYR A 20 38.154 49.694 26.772 1.00 11.40 6 150 C TYR A 20 37.73049.476 25.321 1.00 10.89 6 151 O TYR A 20 36.593 49.813 24.934 1.0011.80 8 152 CB TYR A 20 37.417 48.696 27.719 1.00 12.88 6 153 CG TYR A20 37.927 47.270 27.504 1.00 13.88 6 154 CD1 TYR A 20 39.216 46.96827.943 1.00 14.05 6 155 CD2 TYR A 20 37.160 46.285 26.932 1.00 15.80 6156 CE1 TYR A 20 39.717 45.678 27.800 1.00 16.74 6 157 CE2 TYR A 2037.658 44.982 26.795 1.00 19.32 6 158 CZ TYR A 20 38.935 44.710 27.2141.00 19.70 6 159 OH TYR A 20 39.458 43.422 27.062 1.00 22.69 8 160 N ASPA 21 38.662 48.893 24.586 1.00 13.46 7 161 CA ASP A 21 38.414 48.62823.134 1.00 14.35 6 162 C ASP A 21 37.754 47.226 23.097 1.00 14.61 6 163O ASP A 21 38.426 46.196 23.063 1.00 13.84 8 164 CB ASP A 21 39.74648.665 22.413 1.00 14.54 6 165 CG ASP A 21 39.678 48.444 20.909 1.0017.30 6 166 OD1 ASP A 21 38.565 48.288 20.425 1.00 12.67 8 167 OD2 ASP A21 40.759 48.450 20.282 1.00 15.87 8 168 N GLY A 22 36.430 47.219 23.0401.00 12.11 7 169 CA GLY A 22 35.683 45.934 23.110 1.00 15.21 6 170 C GLYA 22 35.482 45.410 21.664 1.00 18.33 6 171 O GLY A 22 35.034 44.26421.516 1.00 17.21 8 172 N ASP A 23 35.786 46.189 20.639 1.00 13.30 7 173CA ASP A 23 35.505 45.770 19.261 1.00 14.68 6 174 C ASP A 23 36.63446.389 18.425 1.00 14.54 6 175 O ASP A 23 36.570 47.597 18.138 1.0013.39 8 176 CB ASP A 23 34.163 46.271 18.762 1.00 13.59 6 177 CG ASP A23 33.889 45.785 17.319 1.00 16.74 6 178 OD1 ASP A 23 34.805 45.20016.750 1.00 17.96 8 179 OD2 ASP A 23 32.782 46.058 16.872 1.00 16.43 8180 N THR A 24 37.681 45.659 18.083 1.00 15.02 7 181 CA THR A 24 38.76946.308 17.340 1.00 16.37 6 182 C THR A 24 38.381 46.606 15.923 1.0015.39 6 183 O THR A 24 39.124 47.376 15.252 1.00 16.40 8 184 CB THR A 2440.033 45.402 17.367 1.00 18.68 6 185 OG1 THR A 24 39.710 44.147 16.6731.00 17.99 8 186 CG2 THR A 24 40.478 45.112 18.772 1.00 22.45 6 187 NTHR A 25 37.228 46.150 15.423 1.00 16.09 7 188 CA THR A 25 36.864 46.33014.019 1.00 16.07 6 189 C THR A 25 36.349 47.743 13.724 1.00 16.52 6 190O THR A 25 36.215 48.013 12.538 1.00 20.25 8 191 CB THR A 25 35.78045.366 13.475 1.00 20.06 6 192 OG1 THR A 25 34.475 45.532 14.010 1.0018.04 8 193 CG2 THR A 25 36.248 43.924 13.739 1.00 21.26 6 194 N ASN A26 36.066 48.509 14.802 1.00 13.98 7 195 CA ASN A 26 35.577 49.87114.471 1.00 12.49 6 196 C ASN A 26 36.689 50.862 14.772 1.00 13.05 6 197O ASN A 26 36.435 52.053 14.825 1.00 11.58 8 198 CB ASN A 26 34.28350.103 15.246 1.00 13.85 6 199 CG ASN A 26 34.435 49.981 16.739 1.0015.62 6 200 OD1 ASN A 26 35.558 50.066 17.224 1.00 12.89 8 201 ND2 ASN A26 33.339 49.796 17.497 1.00 16.36 7 202 N ASN A 27 37.946 50.401 14.8901.00 14.79 7 203 CA ASN A 27 38.972 51.353 15.290 1.00 12.19 6 204 C ASNA 27 39.404 52.337 14.189 1.00 13.62 6 205 O ASN A 27 39.775 53.46114.499 1.00 14.13 8 206 CB ASN A 27 40.235 50.575 15.662 1.00 12.10 6207 CG ASN A 27 40.150 49.884 17.001 1.00 15.80 6 208 OD1 ASN A 2739.065 49.932 17.554 1.00 12.92 8 209 ND2 ASN A 27 41.187 49.291 17.5711.00 15.14 7 210 N ASN A 28 39.211 51.954 12.920 1.00 14.26 7 211 CA ASNA 28 39.604 52.918 11.854 1.00 15.71 6 212 C ASN A 28 38.672 52.70510.661 1.00 14.39 6 213 O ASN A 28 39.059 52.148 9.622 1.00 16.82 8 214CB ASN A 28 41.036 52.497 11.478 1.00 13.79 6 215 CG ASN A 28 41.79053.538 10.656 1.00 21.29 6 216 OD1 ASN A 28 41.391 54.685 10.535 1.0017.46 8 217 ND2 ASN A 28 42.936 53.086 10.108 1.00 24.72 7 218 N PRO A29 37.442 53.154 10.790 1.00 15.04 7 219 CA PRO A 29 36.430 52.993 9.7421.00 17.37 6 220 C PRO A 29 36.734 53.802 8.507 1.00 18.08 6 221 O PRO A29 37.259 54.906 8.580 1.00 16.51 8 222 CB PRO A 29 35.087 53.483 10.3121.00 17.71 6 223 CG PRO A 29 35.394 53.615 11.787 1.00 17.95 6 224 CDPRO A 29 36.907 53.841 11.957 1.00 15.54 6 225 N ALA A 30 36.329 53.2447.331 1.00 16.99 7 226 CA ALA A 30 36.533 54.024 6.117 1.00 19.06 6 227C ALA A 30 35.841 55.375 6.161 1.00 16.15 6 228 O ALA A 30 36.398 56.3555.599 1.00 18.27 8 229 CB ALA A 30 35.998 53.268 4.880 1.00 21.27 6 230N LYS A 31 34.697 55.514 6.833 1.00 15.01 7 231 CA LYS A 31 34.01256.812 6.886 1.00 14.64 6 232 C LYS A 31 34.944 57.908 7.416 1.00 15.076 233 O LYS A 31 34.722 59.094 7.172 1.00 14.25 8 234 CB LYS A 31 32.77156.667 7.818 1.00 13.99 6 235 CG LYS A 31 31.981 57.980 8.050 1.00 13.236 236 CD LYS A 31 30.617 57.569 8.669 1.00 16.17 6 237 CE LYS A 3129.763 58.766 9.053 1.00 14.65 6 238 NZ LYS A 31 30.427 59.568 10.1561.00 12.05 7 239 N SER A 32 35.822 57.610 8.364 1.00 16.27 7 240 CA SERA 32 36.675 58.587 9.038 1.00 14.39 6 241 C SER A 32 38.087 57.989 9.1611.00 17.62 6 242 O SER A 32 38.770 57.968 10.193 1.00 17.19 8 243 CB SERA 32 36.100 58.851 10.460 1.00 12.32 6 244 OG SER A 32 35.874 57.66411.167 1.00 12.92 8 245 N TYR A 33 38.596 57.524 8.010 1.00 14.71 7 246CA TYR A 33 39.875 56.801 8.045 1.00 15.23 6 247 C TYR A 33 41.05157.676 8.444 1.00 14.94 6 248 O TYR A 33 41.042 58.848 8.023 1.00 17.628 249 CB TYR A 33 40.075 56.295 6.582 1.00 18.09 6 250 CG TYR A 3341.166 55.254 6.536 1.00 20.46 6 251 CD1 TYR A 33 40.982 53.978 7.0041.00 26.95 6 252 CD2 TYR A 33 42.408 55.618 6.002 1.00 31.14 6 253 CE1TYR A 33 41.994 53.027 6.944 1.00 33.56 6 254 CE2 TYR A 33 43.422 54.6705.943 1.00 31.30 6 255 CZ TYR A 33 43.210 53.409 6.402 1.00 33.88 6 256OH TYR A 33 44.235 52.483 6.334 1.00 44.90 8 257 N GLY A 34 42.03957.105 9.114 1.00 12.92 7 258 CA GLY A 34 43.281 57.836 9.403 1.00 14.926 259 C GLY A 34 43.255 58.672 10.686 1.00 15.08 6 260 O GLY A 34 44.27459.342 10.956 1.00 15.24 8 261 N LEU A 35 42.253 58.417 11.548 1.0012.52 7 262 CA LEU A 35 42.215 59.140 12.846 1.00 11.02 6 263 C LEU A 3542.519 58.271 14.028 1.00 15.01 6 264 O LEU A 35 42.472 58.755 15.1821.00 14.18 8 265 CB LEU A 35 40.784 59.737 13.090 1.00 10.53 6 266 CGLEU A 35 40.170 60.460 11.891 1.00 12.89 6 267 CD1 LEU A 35 38.78361.033 12.240 1.00 13.47 6 268 CD2 LEU A 35 41.090 61.613 11.433 1.0015.36 6 269 N TYR A 36 43.025 57.036 13.757 1.00 13.30 7 270 CA TYR A 3643.335 56.061 14.796 1.00 13.00 6 271 C TYR A 36 44.826 55.913 15.0321.00 15.18 6 272 O TYR A 36 45.610 55.855 14.049 1.00 15.86 8 273 CB TYRA 36 42.749 54.728 14.291 1.00 13.61 6 274 CG TYR A 36 43.149 53.49215.076 1.00 12.30 6 275 CD1 TYR A 36 42.927 53.383 16.454 1.00 14.21 6276 CD2 TYR A 36 43.807 52.460 14.391 1.00 16.88 6 277 CE1 TYR A 3643.317 52.206 17.122 1.00 14.97 6 278 CE2 TYR A 36 44.182 51.320 15.0751.00 19.02 6 279 CZ TYR A 36 43.930 51.206 16.416 1.00 17.90 6 280 OHTYR A 36 44.299 50.063 17.135 1.00 18.88 8 281 N ASP A 37 45.211 55.84816.289 1.00 12.45 7 282 CA ASP A 37 46.646 55.624 16.621 1.00 12.80 6283 C ASP A 37 46.700 54.350 17.441 1.00 14.03 6 284 O ASP A 37 46.50754.281 18.673 1.00 13.32 8 285 CB ASP A 37 47.120 56.834 17.463 1.0013.46 6 286 CG ASP A 37 48.543 56.543 17.991 1.00 20.57 6 287 OD1 ASP A37 49.278 55.720 17.366 1.00 17.00 8 288 OD2 ASP A 37 48.902 57.11319.028 1.00 17.32 8 289 N PRO A 38 47.163 53.245 16.821 1.00 15.62 7 290CA PRO A 38 47.375 52.024 17.548 1.00 15.67 6 291 C PRO A 38 48.48452.056 18.558 1.00 15.69 6 292 O PRO A 38 48.513 51.189 19.436 1.0018.95 8 293 CB PRO A 38 47.669 50.946 16.450 1.00 17.01 6 294 CG PRO A38 48.367 51.843 15.437 1.00 18.68 6 295 CD PRO A 38 47.570 53.19215.409 1.00 18.22 6 296 N THR A 39 49.385 53.031 18.514 1.00 15.60 7 297CA THR A 39 50.469 53.080 19.499 1.00 14.85 6 298 C THR A 39 50.12653.773 20.822 1.00 17.68 6 299 O THR A 39 50.961 53.777 21.719 1.0017.01 8 300 CB THR A 39 51.692 53.847 18.947 1.00 19.14 6 301 OG1 THR A39 51.503 55.239 18.723 1.00 16.66 8 302 CG2 THR A 39 52.083 53.23317.573 1.00 22.20 6 303 N LYS A 40 48.983 54.487 20.832 1.00 14.93 7 304CA LYS A 40 48.588 55.225 22.041 1.00 14.22 6 305 C LYS A 40 49.73656.141 22.483 1.00 17.80 6 306 O LYS A 40 50.009 56.348 23.685 1.0017.78 8 307 CB LYS A 40 48.104 54.324 23.207 1.00 19.03 6 308 CG LYS A40 47.023 53.320 22.775 1.00 18.65 6 309 CD LYS A 40 46.535 52.54324.031 1.00 21.38 6 310 CE LYS A 40 45.432 51.573 23.590 1.00 22.34 6311 NZ LYS A 40 45.883 50.563 22.605 1.00 21.85 7 312 N SER A 41 50.30756.831 21.475 1.00 16.33 7 313 CA SER A 41 51.307 57.853 21.746 1.0017.21 6 314 C SER A 41 50.929 59.210 21.203 1.00 16.87 6 315 O SER A 4151.606 60.250 21.492 1.00 16.04 8 316 CB SER A 41 52.714 57.429 21.1981.00 17.96 6 317 OG SER A 41 52.625 57.387 19.782 1.00 20.42 8 318 N LYSA 42 49.895 59.315 20.388 1.00 13.73 7 319 CA LYS A 42 49.446 60.58919.836 1.00 12.77 6 320 C LYS A 42 48.152 60.921 20.603 1.00 13.20 6 321O LYS A 42 47.111 60.351 20.317 1.00 12.98 8 322 CB LYS A 42 49.19360.477 18.321 1.00 14.60 6 323 CG LYS A 42 50.523 60.079 17.606 1.0019.41 6 324 CD LYS A 42 50.228 60.163 16.078 1.00 25.03 6 325 CE LYS A42 51.611 60.340 15.395 1.00 34.65 6 326 NZ LYS A 42 52.071 58.94915.130 1.00 41.02 7 327 N TRP A 43 48.256 61.858 21.565 1.00 11.08 7 328CA TRP A 43 47.235 61.925 22.643 1.00 13.35 6 329 C TRP A 43 45.91562.494 22.162 1.00 11.08 6 330 O TRP A 43 45.002 62.429 22.997 1.0013.47 8 331 CB TRP A 43 47.831 62.848 23.743 1.00 14.15 6 332 CG TRP A43 48.739 61.957 24.592 1.00 12.91 6 333 CD1 TRP A 43 50.014 61.59024.338 1.00 14.88 6 334 CD2 TRP A 43 48.362 61.357 25.845 1.00 12.18 6335 NE1 TRP A 43 50.507 60.770 25.364 1.00 16.61 7 336 CE2 TRP A 4349.467 60.633 26.297 1.00 17.08 6 337 CE3 TRP A 43 47.186 61.367 26.6171.00 13.97 6 338 CZ2 TRP A 43 49.497 59.891 27.501 1.00 19.44 6 339 CZ3TRP A 43 47.223 60.644 27.814 1.00 14.34 6 340 CH2 TRP A 43 48.33359.925 28.265 1.00 15.92 6 341 N LYS A 44 45.846 63.088 20.972 1.0011.78 7 342 CA LYS A 44 44.532 63.606 20.529 1.00 10.59 6 343 C LYS A 4443.959 62.797 19.362 1.00 11.15 6 344 O LYS A 44 43.021 63.227 18.7071.00 11.48 8 345 CB LYS A 44 44.647 65.112 20.097 1.00 11.58 6 346 CGLYS A 44 45.053 65.911 21.382 1.00 11.48 6 347 CD LYS A 44 44.928 67.43521.011 1.00 12.19 6 348 CE LYS A 44 45.254 68.171 22.334 1.00 15.83 6349 NZ LYS A 44 45.125 69.681 22.068 1.00 18.92 7 350 N MET A 45 44.47361.576 19.114 1.00 10.42 7 351 CA MET A 45 43.881 60.686 18.112 1.0012.24 6 352 C MET A 45 42.952 59.664 18.768 1.00 11.36 6 353 O MET A 4543.011 59.512 19.985 1.00 12.88 8 354 CB MET A 45 45.028 59.874 17.4421.00 13.26 6 355 CG AMET A 45 46.067 60.710 16.692 0.50 14.78 6 356 SDAMET A 45 45.379 61.237 15.135 0.50 13.95 16 357 CE AMET A 45 45.72860.040 13.903 0.50 12.41 6 355 CG BMET A 45 45.776 60.960 16.619 0.5011.59 6 356 SD BMET A 45 46.918 60.290 15.431 0.50 16.20 16 357 CE BMETA 45 45.864 59.453 14.271 0.50 18.11 6 358 N TYR A 46 42.122 58.96117.976 1.00 10.91 7 359 CA TYR A 46 41.356 57.880 18.584 1.00 13.29 6360 C TYR A 46 42.263 56.691 18.938 1.00 13.10 6 361 O TYR A 46 43.07656.318 18.094 1.00 12.46 8 362 CB TYR A 46 40.258 57.364 17.660 1.0012.44 6 363 CG TYR A 46 39.031 58.210 17.416 1.00 13.02 6 364 CD1 TYR A46 39.075 59.210 16.436 1.00 11.30 6 365 CD2 TYR A 46 37.846 57.97818.105 1.00 12.45 6 366 CE1 TYR A 46 37.940 59.997 16.146 1.00 12.75 6367 CE2 TYR A 46 36.683 58.746 17.838 1.00 9.77 6 368 CZ TYR A 46 36.78959.707 16.881 1.00 10.60 6 369 OH TYR A 46 35.703 60.490 16.547 1.0011.65 8 370 N TRP A 47 42.097 56.222 20.188 1.00 9.67 7 371 CA TRP A 4742.866 55.089 20.664 1.00 11.50 6 372 C TRP A 47 42.065 53.770 20.5791.00 12.29 6 373 O TRP A 47 42.633 52.676 20.711 1.00 12.20 8 374 CB TRPA 47 43.430 55.285 22.077 1.00 12.80 6 375 CG TRP A 47 44.548 56.31622.086 1.00 10.46 6 376 CD1 TRP A 47 45.068 57.007 21.037 1.00 11.88 6377 CD2 TRP A 47 45.300 56.687 23.218 1.00 10.01 6 378 NE1 TRP A 4746.060 57.853 21.485 1.00 11.36 7 379 CE2 TRP A 47 46.219 57.700 22.8201.00 12.07 6 380 CE3 TRP A 47 45.198 56.392 24.603 1.00 12.09 6 381 CZ2TRP A 47 47.103 58.301 23.715 1.00 13.05 6 382 CZ3 TRP A 47 46.07256.974 25.484 1.00 15.07 6 383 CH2 TRP A 47 47.002 57.939 25.033 1.0016.33 6 384 N GLY A 48 40.752 53.875 20.442 1.00 10.96 7 385 CA GLY A 4839.995 52.631 20.097 1.00 11.53 6 386 C GLY A 48 38.960 52.197 21.1061.00 11.03 6 387 O GLY A 48 38.208 51.215 20.845 1.00 12.01 8 388 N GLYA 49 38.834 52.862 22.221 1.00 12.42 7 389 CA GLY A 49 37.789 52.44323.230 1.00 12.08 6 390 C GLY A 49 36.451 52.679 22.614 1.00 9.81 6 391O GLY A 49 36.173 53.629 21.880 1.00 10.92 8 392 N ASP A 50 35.43351.851 23.065 1.00 10.42 7 393 CA ASP A 50 34.135 51.985 22.429 1.0011.91 6 394 C ASP A 50 32.977 51.516 23.344 1.00 11.85 6 395 O ASP A 5033.188 51.228 24.489 1.00 12.76 8 396 CB ASP A 50 34.148 51.188 21.0941.00 10.66 6 397 CG ASP A 50 34.693 49.790 21.327 1.00 14.50 6 398 OD1ASP A 50 34.446 49.184 22.384 1.00 11.19 8 399 OD2 ASP A 50 35.42549.205 20.532 1.00 11.87 8 400 N LEU A 51 31.762 51.615 22.778 1.0011.80 7 401 CA LEU A 51 30.580 51.320 23.617 1.00 11.32 6 402 C LEU A 5130.568 49.843 23.973 1.00 13.43 6 403 O LEU A 51 30.145 49.499 25.0901.00 11.80 8 404 CB LEU A 51 29.272 51.662 22.869 1.00 12.03 6 405 CGLEU A 51 29.178 53.205 22.638 1.00 11.71 6 406 CD1 LEU A 51 28.03653.389 21.666 1.00 13.88 6 407 CD2 LEU A 51 28.915 53.930 23.954 1.0015.76 6 408 N GLU A 52 30.942 48.987 23.037 1.00 12.67 7 409 CA GLU A 5230.995 47.541 23.443 1.00 12.25 6 410 C GLU A 52 32.024 47.239 24.5161.00 12.73 6 411 O GLU A 52 31.816 46.375 25.382 1.00 13.32 8 412 CB GLUA 52 31.182 46.786 22.122 1.00 16.82 6 413 CG GLU A 52 31.390 45.29822.295 1.00 22.57 6 414 CD GLU A 52 30.227 44.545 22.992 1.00 12.69 6415 OE1 GLU A 52 29.097 45.029 23.005 1.00 17.98 8 416 OE2 GLU A 5230.680 43.475 23.419 1.00 16.49 8 417 N GLY A 53 33.114 48.012 24.6281.00 12.03 7 418 CA GLY A 53 34.108 47.857 25.680 1.00 13.18 6 419 C GLYA 53 33.471 48.292 27.005 1.00 12.67 6 420 O GLY A 53 33.737 47.58628.000 1.00 11.91 8 421 N VAL A 54 32.653 49.355 27.005 1.00 11.80 7 422CA VAL A 54 31.996 49.680 28.280 1.00 10.05 6 423 C VAL A 54 31.07848.502 28.715 1.00 12.37 6 424 O VAL A 54 31.055 48.111 29.879 1.0012.15 8 425 CB VAL A 54 31.154 50.947 28.220 1.00 11.03 6 426 CG1 VAL A54 30.449 51.255 29.552 1.00 13.86 6 427 CG2 VAL A 54 32.100 52.14327.853 1.00 11.86 6 428 N ARG A 55 30.387 47.952 27.708 1.00 9.95 7 429CA ARG A 55 29.382 46.875 28.101 1.00 13.29 6 430 C ARG A 55 30.11245.671 28.652 1.00 12.91 6 431 O ARG A 55 29.684 44.943 29.596 1.0013.96 8 432 CB ARG A 55 28.627 46.458 26.819 1.00 13.43 6 433 CG ARG A55 27.364 45.611 27.165 1.00 13.64 6 434 CD ARG A 55 26.723 44.97425.877 1.00 13.15 6 435 NE ARG A 55 27.745 44.040 25.358 1.00 13.30 7436 CZ ARG A 55 28.117 42.905 25.921 1.00 14.35 6 437 NH1 ARG A 5527.475 42.404 27.011 1.00 15.82 7 438 NH2 ARG A 55 29.125 42.171 25.4461.00 17.12 7 439 N GLN A 56 31.265 45.354 28.031 1.00 11.75 7 440 CA GLNA 56 32.050 44.171 28.503 1.00 12.69 6 441 C GLN A 56 32.530 44.33929.945 1.00 14.76 6 442 O GLN A 56 32.895 43.338 30.611 1.00 15.16 8 443CB GLN A 56 33.249 43.948 27.536 1.00 12.12 6 444 CG GLN A 56 32.71843.310 26.223 1.00 12.45 6 445 CD GLN A 56 33.748 43.189 25.110 1.0018.74 6 446 OE1 GLN A 56 33.441 43.161 23.879 1.00 21.22 8 447 NE2 GLN A56 34.957 43.066 25.540 1.00 13.29 7 448 N LYS A 57 32.816 45.574 30.3551.00 13.93 7 449 CA LYS A 57 33.243 45.881 31.703 1.00 11.77 6 450 C LYSA 57 32.146 46.200 32.702 1.00 13.05 6 451 O LYS A 57 32.397 46.65133.834 1.00 12.11 8 452 CB LYS A 57 34.240 47.112 31.625 1.00 12.27 6453 CG LYS A 57 35.508 46.752 30.818 1.00 13.15 6 454 CD LYS A 57 36.16745.442 31.318 1.00 13.38 6 455 CE LYS A 57 37.577 45.277 30.729 1.0016.88 6 456 NZ LYS A 57 38.170 43.960 31.261 1.00 17.21 7 457 N LEU A 5830.883 45.891 32.388 1.00 12.90 7 458 CA LEU A 58 29.789 46.048 33.3381.00 14.31 6 459 C LEU A 58 29.981 45.299 34.668 1.00 12.68 6 460 O LEUA 58 29.737 45.865 35.732 1.00 13.94 8 461 CB LEU A 58 28.407 45.77932.723 1.00 12.52 6 462 CG LEU A 58 27.963 46.878 31.718 1.00 12.14 6463 CD1 LEU A 58 26.709 46.366 30.943 1.00 14.87 6 464 CD2 LEU A 5827.586 48.136 32.488 1.00 15.84 6 465 N PRO A 59 30.555 44.107 34.6701.00 13.13 7 466 CA PRO A 59 30.776 43.396 35.937 1.00 14.64 6 467 C PROA 59 31.759 44.139 36.827 1.00 14.63 6 468 O PRO A 59 31.532 44.25038.038 1.00 15.79 8 469 CB PRO A 59 31.436 42.034 35.525 1.00 15.40 6470 CG PRO A 59 30.719 41.845 34.161 1.00 16.79 6 471 CD PRO A 59 30.80743.247 33.514 1.00 16.71 6 472 N TYR A 60 32.806 44.717 36.210 1.0012.89 7 473 CA TYR A 60 33.789 45.511 36.994 1.00 12.47 6 474 C TYR A 6033.072 46.731 37.584 1.00 12.64 6 475 O TYR A 60 33.237 46.994 38.7971.00 13.63 8 476 CB TYR A 60 34.918 45.920 36.026 1.00 12.16 6 477 CGTYR A 60 35.856 46.938 36.667 1.00 12.17 6 478 CD1 TYR A 60 36.91746.528 37.462 1.00 13.23 6 479 CD2 TYR A 60 35.602 48.293 36.453 1.0012.24 6 480 CE1 TYR A 60 37.730 47.509 38.049 1.00 12.99 6 481 CE2 TYR A60 36.438 49.268 37.022 1.00 14.93 6 482 CZ TYR A 60 37.473 48.85237.823 1.00 14.75 6 483 OH TYR A 60 38.287 49.782 38.464 1.00 13.93 8484 N LEU A 61 32.298 47.410 36.735 1.00 11.74 7 485 CA LEU A 61 31.62248.610 37.225 1.00 11.91 6 486 C LEU A 61 30.570 48.316 38.272 1.0014.11 6 487 O LEU A 61 30.508 49.022 39.283 1.00 13.33 8 488 CB LEU A 6130.993 49.382 36.051 1.00 12.06 6 489 CG LEU A 61 32.030 49.809 34.9921.00 13.18 6 490 CD1 LEU A 61 31.263 50.310 33.753 1.00 15.35 6 491 CD2LEU A 61 32.865 50.971 35.605 1.00 16.34 6 492 N LYS A 62 29.850 47.21738.162 1.00 12.47 7 493 CA LYS A 62 28.890 46.844 39.202 1.00 13.25 6494 C LYS A 62 29.614 46.558 40.535 1.00 13.60 6 495 O LYS A 62 29.14947.032 41.576 1.00 15.97 8 496 CB LYS A 62 28.117 45.588 38.730 1.0014.71 6 497 CG LYS A 62 27.011 45.263 39.764 1.00 17.27 6 498 CD LYS A62 25.908 44.363 39.223 1.00 30.17 6 499 CE LYS A 62 24.879 44.08840.343 1.00 25.52 6 500 NZ LYS A 62 23.887 45.203 40.515 1.00 24.63 7501 N GLN A 63 30.722 45.781 40.455 1.00 12.05 7 502 CA GLN A 63 31.43745.448 41.660 1.00 10.80 6 503 C GLN A 63 32.010 46.705 42.325 1.0013.71 6 504 O GLN A 63 32.200 46.751 43.544 1.00 13.66 8 505 CB AGLN A63 32.582 44.501 41.262 0.66 17.93 6 506 CG AGLN A 63 32.178 43.09240.865 0.66 27.01 6 507 CD AGLN A 63 33.421 42.362 40.343 0.66 35.95 6508 OE1 AGLN A 63 34.283 42.022 41.149 0.66 40.99 8 509 NE2 AGLN A 6333.525 42.128 39.043 0.66 36.04 7 505 CB BGLN A 63 32.511 44.387 41.3450.33 7.59 6 506 CG BGLN A 63 33.072 43.793 42.621 0.33 8.29 6 507 CDBGLN A 63 34.234 42.824 42.408 0.33 8.28 6 508 OE1 BGLN A 63 34.48042.416 41.279 0.33 14.24 8 509 NE2 BGLN A 63 34.884 42.519 43.537 0.3312.44 7 510 N LEU A 64 32.481 47.646 41.498 1.00 10.99 7 511 CA LEU A 6432.993 48.909 42.087 1.00 15.73 6 512 C LEU A 64 31.893 49.656 42.8371.00 14.21 6 513 O LEU A 64 32.253 50.516 43.659 1.00 14.81 8 514 CB LEUA 64 33.536 49.777 40.930 1.00 14.15 6 515 CG LEU A 64 34.050 51.20141.274 1.00 13.04 6 516 CD1 LEU A 64 35.177 51.132 42.303 1.00 12.46 6517 CD2 LEU A 64 34.587 51.825 39.963 1.00 12.70 6 518 N GLY A 65 30.60549.492 42.566 1.00 14.23 7 519 CA GLY A 65 29.537 50.247 43.205 1.0013.78 6 520 C GLY A 65 28.987 51.337 42.311 1.00 14.56 6 521 O GLY A 6528.207 52.222 42.758 1.00 13.13 8 522 N VAL A 66 29.343 51.265 41.0141.00 12.13 7 523 CA VAL A 66 28.773 52.267 40.114 1.00 10.77 6 524 C VALA 66 27.297 52.007 39.842 1.00 13.82 6 525 O VAL A 66 26.933 50.83639.617 1.00 13.38 8 526 CB VAL A 66 29.491 52.192 38.744 1.00 11.10 6527 CG1 VAL A 66 28.892 53.220 37.731 1.00 12.12 6 528 CG2 VAL A 6630.961 52.489 38.974 1.00 14.48 6 529 N THR A 67 26.431 53.016 39.9921.00 10.70 7 530 CA THR A 67 25.022 52.822 39.675 1.00 12.22 6 531 C THRA 67 24.526 53.737 38.565 1.00 13.77 6 532 O THR A 67 23.404 53.53838.103 1.00 13.29 8 533 CB THR A 67 24.072 52.926 40.898 1.00 14.25 6534 OG1 THR A 67 24.680 53.791 41.874 1.00 13.89 8 535 CG2 THR A 6724.085 51.519 41.584 1.00 14.96 6 536 N THR A 68 25.351 54.723 38.1561.00 12.63 7 537 CA THR A 68 25.042 55.479 36.914 1.00 10.68 6 538 C THRA 68 26.379 55.684 36.193 1.00 9.37 6 539 O THR A 68 27.313 56.21436.775 1.00 11.86 8 540 CB THR A 68 24.388 56.837 37.236 1.00 13.89 6541 OG1 THR A 68 23.094 56.649 37.793 1.00 13.19 8 542 CG2 THR A 6824.269 57.734 35.965 1.00 14.32 6 543 N ILE A 69 26.394 55.287 34.8961.00 9.42 7 544 CA ILE A 69 27.605 55.600 34.073 1.00 8.17 6 545 C ILE A69 27.249 56.897 33.377 1.00 11.16 6 546 O ILE A 69 26.200 57.080 32.7341.00 12.50 8 547 CB ILE A 69 27.714 54.510 32.986 1.00 12.66 6 548 CG1ILE A 69 28.160 53.214 33.736 1.00 14.05 6 549 CG2 ILE A 69 28.73754.893 31.900 1.00 11.22 6 550 CD1 ILE A 69 27.937 52.008 32.775 1.0013.93 6 551 N TRP A 70 28.196 57.872 33.425 1.00 9.74 7 552 CA TRP A 7028.095 59.093 32.600 1.00 10.34 6 553 C TRP A 70 28.991 58.790 31.4031.00 11.63 6 554 O TRP A 70 30.214 58.751 31.558 1.00 11.51 8 555 CB TRPA 70 28.494 60.327 33.441 1.00 9.83 6 556 CG TRP A 70 28.954 61.55832.738 1.00 8.81 6 557 CD1 TRP A 70 29.050 61.770 31.360 1.00 13.03 6558 CD2 TRP A 70 29.591 62.698 33.356 1.00 10.57 6 559 NE1 TRP A 7029.645 63.016 31.118 1.00 12.41 7 560 CE2 TRP A 70 30.017 63.558 32.3381.00 10.48 6 561 CE3 TRP A 70 29.830 63.007 34.699 1.00 12.18 6 562 CZ2TRP A 70 30.721 64.729 32.587 1.00 9.61 6 563 CZ3 TRP A 70 30.426 64.23434.950 1.00 11.62 6 564 CH2 TRP A 70 30.896 65.061 33.914 1.00 13.98 6565 N LEU A 71 28.373 58.542 30.225 1.00 10.83 7 566 CA LEU A 71 29.21958.311 29.023 1.00 11.92 6 567 C LEU A 71 29.585 59.691 28.439 1.0010.49 6 568 O LEU A 71 28.669 60.552 28.276 1.00 10.64 8 569 CB LEU A 7128.342 57.617 27.923 1.00 11.13 6 570 CG LEU A 71 27.991 56.159 28.2401.00 11.31 6 571 CD1 LEU A 71 27.073 55.665 27.096 1.00 10.98 6 572 CD2LEU A 71 29.253 55.314 28.322 1.00 11.96 6 573 N SER A 72 30.870 59.86528.066 1.00 10.17 7 574 CA SER A 72 31.250 60.995 27.218 1.00 9.81 6 575C SER A 72 30.455 60.988 25.920 1.00 11.22 6 576 O SER A 72 29.73360.011 25.572 1.00 10.33 8 577 CB SER A 72 32.773 60.898 26.944 1.0010.62 6 578 OG SER A 72 33.092 59.694 26.237 1.00 11.62 8 579 N PRO A 7330.447 62.034 25.128 1.00 11.10 7 580 CA PRO A 73 29.427 62.188 24.0481.00 11.86 6 581 C PRO A 73 29.521 61.057 23.042 1.00 13.54 6 582 O PROA 73 30.653 60.649 22.674 1.00 11.75 8 583 CB PRO A 73 29.672 63.56323.414 1.00 10.32 6 584 CG PRO A 73 30.360 64.313 24.557 1.00 10.23 6585 CD PRO A 73 31.228 63.286 25.358 1.00 11.09 6 586 N VAL A 74 28.34560.538 22.623 1.00 11.02 7 587 CA VAL A 74 28.351 59.338 21.794 1.009.14 6 588 C VAL A 74 27.998 59.628 20.344 1.00 9.79 6 589 O VAL A 7428.041 58.700 19.549 1.00 10.96 8 590 CB VAL A 74 27.260 58.313 22.3111.00 9.29 6 591 CG1 VAL A 74 27.541 57.935 23.780 1.00 11.66 6 592 CG2VAL A 74 25.882 58.894 22.161 1.00 10.26 6 593 N LEU A 75 27.708 60.91219.980 1.00 10.62 7 594 CA LEU A 75 27.182 61.136 18.619 1.00 10.48 6595 C LEU A 75 28.305 61.464 17.620 1.00 12.02 6 596 O LEU A 75 29.43661.678 18.016 1.00 11.28 8 597 CB LEU A 75 26.111 62.279 18.660 1.0010.81 6 598 CG LEU A 75 24.952 61.966 19.634 1.00 11.49 6 599 CD1 LEU A75 24.074 63.178 19.911 1.00 11.47 6 600 CD2 LEU A 75 24.074 60.86418.960 1.00 11.05 6 601 N ASP A 76 27.958 61.296 16.347 1.00 10.11 7 602CA ASP A 76 29.020 61.292 15.299 1.00 9.23 6 603 C ASP A 76 29.82162.605 15.351 1.00 9.60 6 604 O ASP A 76 29.263 63.683 15.155 1.00 11.118 605 CB ASP A 76 28.264 61.153 13.979 1.00 9.89 6 606 CG ASP A 7629.177 61.079 12.745 1.00 12.56 6 607 OD1 ASP A 76 30.380 60.856 12.8951.00 12.97 8 608 OD2 ASP A 76 28.617 61.239 11.641 1.00 11.97 8 609 NASN A 77 31.131 62.435 15.524 1.00 9.80 7 610 CA ASN A 77 32.043 63.57015.534 1.00 9.86 6 611 C ASN A 77 32.766 63.691 14.180 1.00 10.69 6 612O ASN A 77 32.797 62.759 13.385 1.00 10.51 8 613 CB ASN A 77 33.11763.370 16.619 1.00 10.13 6 614 CG ASN A 77 32.685 63.988 17.945 1.0013.40 6 615 OD1 ASN A 77 33.515 64.636 18.600 1.00 10.92 8 616 ND2 ASN A77 31.412 63.908 18.341 1.00 11.73 7 617 N LEU A 78 33.296 64.886 13.9671.00 10.62 7 618 CA LEU A 78 34.240 65.195 12.866 1.00 11.24 6 619 C LEUA 78 34.929 63.977 12.309 1.00 8.87 6 620 O LEU A 78 35.632 63.25713.026 1.00 12.04 8 621 CB LEU A 78 35.257 66.197 13.506 1.00 9.81 6 622CG LEU A 78 36.289 66.679 12.399 1.00 9.30 6 623 CD1 LEU A 78 35.62267.597 11.418 1.00 11.34 6 624 CD2 LEU A 78 37.382 67.439 13.176 1.0013.04 6 625 N ASP A 79 34.801 63.867 10.945 1.00 11.36 7 626 CA ASP A 7935.393 62.670 10.348 1.00 9.32 6 627 C ASP A 79 36.754 62.947 9.688 1.0012.70 6 628 O ASP A 79 37.275 62.042 9.026 1.00 14.30 8 629 CB ASP A 7934.468 62.189 9.168 1.00 14.19 6 630 CG ASP A 79 33.217 61.518 9.6581.00 15.14 6 631 OD1 ASP A 79 33.208 61.150 10.841 1.00 12.50 8 632 OD2ASP A 79 32.239 61.307 8.931 1.00 12.26 8 633 N THR A 80 37.307 64.1159.950 1.00 12.57 7 634 CA THR A 80 38.652 64.479 9.456 1.00 14.13 6 635C THR A 80 39.521 64.930 10.635 1.00 13.16 6 636 O THR A 80 39.07264.981 11.769 1.00 12.58 8 637 CB THR A 80 38.583 65.712 8.534 1.0014.19 6 638 OG1 THR A 80 38.265 66.927 9.264 1.00 15.46 8 639 CG2 THR A80 37.593 65.645 7.372 1.00 19.78 6 640 N LEU A 81 40.809 65.216 10.3271.00 13.37 7 641 CA LEU A 81 41.651 65.864 11.341 1.00 10.22 6 642 C LEUA 81 41.263 67.297 11.488 1.00 12.10 6 643 O LEU A 81 40.635 67.90010.595 1.00 12.72 8 644 CB LEU A 81 43.143 65.818 10.830 1.00 10.42 6645 CG LEU A 81 43.643 64.345 10.809 1.00 15.27 6 646 CD1 LEU A 8144.897 64.351 9.927 1.00 21.14 6 647 CD2 LEU A 81 44.059 63.885 12.2441.00 14.05 6 648 N ALA A 82 41.647 67.888 12.629 1.00 11.74 7 649 CA ALAA 82 41.548 69.320 12.798 1.00 13.34 6 650 C ALA A 82 42.941 69.80113.202 1.00 12.91 6 651 O ALA A 82 43.208 70.247 14.316 1.00 11.11 8 652CB ALA A 82 40.566 69.586 13.989 1.00 14.40 6 653 N GLY A 83 43.81169.835 12.180 1.00 12.89 7 654 CA GLY A 83 45.245 70.145 12.484 1.0011.52 6 655 C GLY A 83 45.960 68.860 12.923 1.00 12.02 6 656 O GLY A 8345.405 67.737 13.060 1.00 11.47 8 657 N THR A 84 47.262 68.987 13.2301.00 12.31 7 658 CA THR A 84 48.160 67.879 13.444 1.00 11.91 6 659 C THRA 84 47.716 66.883 14.496 1.00 10.74 6 660 O THR A 84 47.554 67.21315.687 1.00 11.33 8 661 CB THR A 84 49.570 68.477 13.888 1.00 10.32 6662 OG1 THR A 84 49.942 69.432 12.873 1.00 12.17 8 663 CG2 THR A 8450.533 67.298 14.074 1.00 13.58 6 664 N ASP A 85 47.462 65.652 14.0191.00 12.06 7 665 CA ASP A 85 47.117 64.552 14.933 1.00 10.80 6 666 C ASPA 85 45.981 64.902 15.894 1.00 12.31 6 667 O ASP A 85 45.986 64.41617.030 1.00 13.43 8 668 CB ASP A 85 48.356 64.077 15.747 1.00 14.44 6669 CG ASP A 85 49.500 63.600 14.831 1.00 22.31 6 670 OD1 ASP A 8549.284 63.065 13.744 1.00 14.91 8 671 OD2 ASP A 85 50.645 63.782 15.2751.00 23.25 8 672 N ASN A 86 45.024 65.712 15.418 1.00 10.53 7 673 CA ASNA 86 44.024 66.196 16.401 1.00 10.12 6 674 C ASN A 86 42.644 65.78415.880 1.00 9.75 6 675 O ASN A 86 42.241 66.073 14.747 1.00 12.30 8 676CB ASN A 86 44.190 67.732 16.468 1.00 11.52 6 677 CG ASN A 86 43.47068.295 17.677 1.00 13.68 6 678 OD1 ASN A 86 42.743 67.535 18.341 1.0014.08 8 679 ND2 ASN A 86 43.644 69.546 18.063 1.00 15.21 7 680 N THR A87 41.877 65.099 16.705 1.00 10.11 7 681 CA THR A 87 40.619 64.45916.251 1.00 10.70 6 682 C THR A 87 39.525 64.643 17.317 1.00 11.84 6 683O THR A 87 39.764 65.021 18.471 1.00 11.11 8 684 CB THR A 87 40.74562.924 16.124 1.00 12.30 6 685 OG1 THR A 87 40.840 62.298 17.444 1.0011.34 8 686 CG2 THR A 87 41.961 62.467 15.375 1.00 11.19 6 687 N GLY A88 38.307 64.357 16.903 1.00 11.28 7 688 CA GLY A 88 37.184 64.32917.887 1.00 10.27 6 689 C GLY A 88 37.107 63.063 18.721 1.00 10.54 6 690O GLY A 88 35.954 62.712 19.121 1.00 10.21 8 691 N TYR A 89 38.19662.404 19.087 1.00 10.33 7 692 CA TYR A 89 38.134 61.241 19.955 1.0010.06 6 693 C TYR A 89 37.314 61.476 21.204 1.00 11.70 6 694 O TYR A 8936.760 60.489 21.732 1.00 11.42 8 695 CB TYR A 89 39.564 60.769 20.3161.00 9.10 6 696 CG TYR A 89 40.152 61.653 21.412 1.00 11.07 6 697 CD1TYR A 89 40.732 62.857 21.106 1.00 10.61 6 698 CD2 TYR A 89 40.05861.256 22.750 1.00 9.12 6 699 CE1 TYR A 89 41.243 63.688 22.115 1.009.21 6 700 CE2 TYR A 89 40.505 62.054 23.777 1.00 11.90 6 701 CZ TYR A89 41.098 63.267 23.443 1.00 10.92 6 702 OH TYR A 89 41.593 64.12624.411 1.00 10.82 8 703 N HIS A 90 37.283 62.703 21.748 1.00 10.85 7 704CA HIS A 90 36.623 62.983 23.011 1.00 9.54 6 705 C HIS A 90 35.09563.104 22.837 1.00 7.69 6 706 O HIS A 90 34.392 63.040 23.856 1.00 9.028 707 CB HIS A 90 37.178 64.338 23.555 1.00 10.73 6 708 CG HIS A 9037.294 65.403 22.507 1.00 11.48 6 709 ND1 HIS A 90 36.210 66.035 21.9261.00 9.73 7 710 CD2 HIS A 90 38.405 65.898 21.906 1.00 8.93 6 711 CE1HIS A 90 36.686 66.903 21.010 1.00 10.94 6 712 NE2 HIS A 90 37.98866.862 20.995 1.00 10.18 7 713 N GLY A 91 34.616 63.356 21.629 1.00 9.667 714 CA GLY A 91 33.143 63.393 21.404 1.00 9.79 6 715 C GLY A 91 32.50564.768 21.395 1.00 10.82 6 716 O GLY A 91 31.287 64.916 21.102 1.0011.09 8 717 N TYR A 92 33.288 65.840 21.633 1.00 10.15 7 718 CA TYR A 9232.653 67.152 21.753 1.00 10.44 6 719 C TYR A 92 32.556 67.935 20.4591.00 8.85 6 720 O TYR A 92 32.132 69.141 20.520 1.00 9.64 8 721 CB TYR A92 33.461 67.977 22.837 1.00 10.08 6 722 CG TYR A 92 33.217 67.38524.219 1.00 10.98 6 723 CD1 TYR A 92 32.091 67.719 24.974 1.00 10.25 6724 CD2 TYR A 92 34.112 66.472 24.730 1.00 10.46 6 725 CE1 TYR A 9231.905 67.143 26.247 1.00 10.96 6 726 CE2 TYR A 92 33.932 65.888 25.9831.00 14.14 6 727 CZ TYR A 92 32.829 66.237 26.715 1.00 11.56 6 728 OHTYR A 92 32.648 65.665 27.970 1.00 12.31 8 729 N TRP A 93 32.968 67.34319.345 1.00 10.19 7 730 CA TRP A 93 32.914 68.040 18.039 1.00 11.73 6731 C TRP A 93 31.949 67.307 17.103 1.00 9.84 6 732 O TRP A 93 32.33666.443 16.294 1.00 10.83 8 733 CB TRP A 93 34.322 68.024 17.415 1.0012.42 6 734 CG TRP A 93 35.359 68.775 18.253 1.00 11.75 6 735 CD1 TRP A93 35.181 69.659 19.258 1.00 12.58 6 736 CD2 TRP A 93 36.786 68.65718.020 1.00 11.96 6 737 NE1 TRP A 93 36.448 70.120 19.694 1.00 13.60 7738 CE2 TRP A 93 37.397 69.501 18.932 1.00 14.78 6 739 CE3 TRP A 9337.559 67.884 17.130 1.00 13.74 6 740 CZ2 TRP A 93 38.808 69.626 19.0401.00 15.96 6 741 CZ3 TRP A 93 38.959 68.021 17.209 1.00 10.95 6 742 CH2TRP A 93 39.526 68.880 18.171 1.00 9.91 6 743 N THR A 94 30.669 67.53417.237 1.00 10.45 7 744 CA THR A 94 29.603 66.690 16.661 1.00 9.91 6 745C THR A 94 29.244 67.242 15.270 1.00 11.32 6 746 O THR A 94 28.85468.415 15.074 1.00 11.48 8 747 CB THR A 94 28.302 66.837 17.495 1.009.85 6 748 OG1 THR A 94 28.643 66.563 18.891 1.00 11.49 8 749 CG2 THR A94 27.263 65.739 17.079 1.00 11.23 6 750 N ARG A 95 29.315 66.299 14.2921.00 10.33 7 751 CA ARG A 95 28.819 66.623 12.945 1.00 11.51 6 752 C ARGA 95 27.382 66.123 12.703 1.00 13.19 6 753 O ARG A 95 26.834 66.52311.700 1.00 12.00 8 754 CB ARG A 95 29.766 65.999 11.920 1.00 12.95 6755 CG ARG A 95 29.739 64.437 11.900 1.00 9.03 6 756 CD ARG A 95 30.89463.964 11.008 1.00 12.99 6 757 NE ARG A 95 30.917 64.346 9.584 1.0013.10 7 758 CZ ARG A 95 30.216 63.680 8.633 1.00 13.74 6 759 NH1 ARG A95 29.307 62.746 8.918 1.00 13.30 7 760 NH2 ARG A 95 30.477 64.026 7.3801.00 15.12 7 761 N ASP A 96 26.880 65.176 13.503 1.00 11.44 7 762 CA ASPA 96 25.536 64.640 13.218 1.00 11.75 6 763 C ASP A 96 24.977 64.16614.570 1.00 10.37 6 764 O ASP A 96 25.448 63.154 15.091 1.00 12.67 8 765CB ASP A 96 25.622 63.467 12.217 1.00 10.69 6 766 CG ASP A 96 24.23863.012 11.732 1.00 14.77 6 767 OD1 ASP A 96 23.229 63.251 12.412 1.0011.10 8 768 OD2 ASP A 96 24.218 62.343 10.651 1.00 15.82 8 769 N PHE A97 24.007 64.989 15.033 1.00 9.84 7 770 CA PHE A 97 23.482 64.615 16.3771.00 10.91 6 771 C PHE A 97 22.504 63.426 16.336 1.00 13.19 6 772 O PHEA 97 21.945 63.125 17.373 1.00 13.15 8 773 CB PHE A 97 22.818 65.84416.982 1.00 10.58 6 774 CG PHE A 97 23.783 66.935 17.422 1.00 14.29 6775 CD1 PHE A 97 24.438 67.807 16.532 1.00 13.03 6 776 CD2 PHE A 9723.979 67.062 18.799 1.00 13.39 6 777 CE1 PHE A 97 25.321 68.786 17.0671.00 11.37 6 778 CE2 PHE A 97 24.780 68.073 19.296 1.00 9.92 6 779 CZPHE A 97 25.489 68.930 18.467 1.00 9.67 6 780 N LYS A 98 22.220 62.88915.152 1.00 11.59 7 781 CA LYS A 98 21.249 61.786 15.105 1.00 10.99 6782 C LYS A 98 21.893 60.424 14.982 1.00 13.58 6 783 O LYS A 98 21.13659.437 14.991 1.00 14.00 8 784 CB LYS A 98 20.375 61.999 13.835 1.0010.72 6 785 CG LYS A 98 19.595 63.337 13.915 1.00 11.63 6 786 CD LYS A98 18.627 63.408 15.091 1.00 16.21 6 787 CE LYS A 98 17.808 64.70715.036 1.00 16.03 6 788 NZ LYS A 98 16.876 64.605 13.828 1.00 15.90 7789 N GLN A 99 23.233 60.336 14.853 1.00 9.90 7 790 CA GLN A 99 23.90059.079 14.613 1.00 11.53 6 791 C GLN A 99 25.042 58.866 15.625 1.0012.11 6 792 O GLN A 99 25.610 59.842 16.118 1.00 13.41 8 793 CB GLN A 9924.657 58.975 13.225 1.00 13.31 6 794 CG GLN A 99 23.575 58.962 12.1371.00 20.81 6 795 CD GLN A 99 24.005 57.830 11.187 1.00 47.61 6 796 OE1GLN A 99 23.966 56.639 11.540 1.00 38.44 8 797 NE2 GLN A 99 24.43558.330 10.031 1.00 51.18 7 798 N ILE A 100 25.139 57.581 16.003 1.0011.97 7 799 CA ILE A 100 26.265 57.291 16.916 1.00 9.69 6 800 C ILE A100 27.586 57.395 16.160 1.00 11.29 6 801 O ILE A 100 27.744 57.03214.974 1.00 13.58 8 802 CB ILE A 100 26.080 55.834 17.385 1.00 11.20 6803 CG1 ILE A 100 24.767 55.651 18.197 1.00 13.05 6 804 CG2 ILE A 10027.229 55.284 18.240 1.00 10.14 6 805 CD1 ILE A 100 24.692 56.541 19.4891.00 13.82 6 806 N GLU A 101 28.607 57.861 16.898 1.00 11.66 7 807 CAGLU A 101 29.968 57.886 16.322 1.00 11.19 6 808 C GLU A 101 30.44356.478 15.956 1.00 11.88 6 809 O GLU A 101 30.430 55.545 16.758 1.0012.38 8 810 CB GLU A 101 30.918 58.478 17.400 1.00 11.53 6 811 CG GLU A101 32.427 58.256 17.126 1.00 10.12 6 812 CD GLU A 101 32.796 58.79115.715 1.00 10.82 6 813 OE1 GLU A 101 32.328 59.903 15.389 1.00 11.74 8814 OE2 GLU A 101 33.577 58.059 15.099 1.00 12.29 8 815 N GLU A 10230.874 56.411 14.662 1.00 12.51 7 816 CA GLU A 102 31.192 55.081 14.1161.00 11.29 6 817 C GLU A 102 32.387 54.443 14.766 1.00 12.50 6 818 O GLUA 102 32.460 53.176 14.813 1.00 11.57 8 819 CB GLU A 102 31.402 55.18212.553 1.00 11.80 6 820 CG GLU A 102 32.656 55.982 12.107 1.00 12.52 6821 CD GLU A 102 32.465 57.475 12.181 1.00 12.69 6 822 OE1 GLU A 10231.368 58.018 12.431 1.00 14.09 8 823 OE2 GLU A 102 33.493 58.174 11.9301.00 15.94 8 824 N HIS A 103 33.391 55.145 15.324 1.00 9.73 7 825 CA HISA 103 34.429 54.494 16.120 1.00 9.99 6 826 C HIS A 103 33.862 53.87417.376 1.00 11.88 6 827 O HIS A 103 34.531 52.943 17.864 1.00 12.86 8828 CB HIS A 103 35.470 55.578 16.584 1.00 12.93 6 829 CG HIS A 10336.364 56.049 15.481 1.00 11.28 6 830 ND1 HIS A 103 36.015 57.085 14.6391.00 12.54 7 831 CD2 HIS A 103 37.595 55.655 15.123 1.00 14.43 6 832 CE1HIS A 103 37.021 57.288 13.749 1.00 13.58 6 833 NE2 HIS A 103 37.96556.434 14.054 1.00 13.95 7 834 N PHE A 104 32.662 54.253 17.819 1.009.60 7 835 CA PHE A 104 32.171 53.727 19.103 1.00 10.30 6 836 C PHE A104 31.116 52.625 18.924 1.00 13.76 6 837 O PHE A 104 30.969 51.85119.894 1.00 13.23 8 838 CB PHE A 104 31.583 54.855 19.953 1.00 10.00 6839 CG PHE A 104 32.587 55.933 20.330 1.00 13.59 6 840 CD1 PHE A 10433.954 55.782 20.204 1.00 11.92 6 841 CD2 PHE A 104 32.082 57.130 20.8341.00 13.49 6 842 CE1 PHE A 104 34.854 56.802 20.561 1.00 12.32 6 843 CE2PHE A 104 32.981 58.161 21.193 1.00 11.48 6 844 CZ PHE A 104 34.36558.005 21.053 1.00 13.46 6 845 N GLY A 105 30.491 52.584 17.759 1.0014.42 7 846 CA GLY A 105 29.462 51.533 17.546 1.00 16.52 6 847 C GLY A105 28.362 52.143 16.670 1.00 17.63 6 848 O GLY A 105 28.624 53.10415.927 1.00 14.43 8 849 N ASN A 106 27.169 51.558 16.664 1.00 14.15 7850 CA ASN A 106 26.017 52.150 15.960 1.00 11.27 6 851 C ASN A 10624.864 52.149 16.958 1.00 13.27 6 852 O ASN A 106 25.081 51.890 18.1741.00 13.00 8 853 CB ASN A 106 25.756 51.332 14.677 1.00 13.55 6 854 CGASN A 106 25.465 49.876 14.958 1.00 18.28 6 855 OD1 ASN A 106 25.09349.459 16.033 1.00 17.05 8 856 ND2 ASN A 106 25.576 49.021 13.910 1.0022.96 7 857 N TRP A 107 23.668 52.508 16.525 1.00 12.62 7 858 CA TRP A107 22.554 52.559 17.465 1.00 13.67 6 859 C TRP A 107 22.296 51.20318.121 1.00 14.10 6 860 O TRP A 107 21.827 51.121 19.274 1.00 14.66 8861 CB TRP A 107 21.268 53.087 16.802 1.00 14.53 6 862 CG TRP A 10721.256 54.576 16.836 1.00 16.29 6 863 CD1 TRP A 107 21.351 55.357 15.6961.00 17.56 6 864 CD2 TRP A 107 21.131 55.454 17.949 1.00 15.71 6 865 NE1TRP A 107 21.279 56.677 16.088 1.00 16.73 7 866 CE2 TRP A 107 21.18656.759 17.451 1.00 14.24 6 867 CE3 TRP A 107 20.995 55.256 19.345 1.0013.30 6 868 CZ2 TRP A 107 21.082 57.915 18.240 1.00 14.74 6 869 CZ3 TRPA 107 20.919 56.410 20.131 1.00 16.80 6 870 CH2 TRP A 107 20.927 57.71719.596 1.00 13.00 6 871 N THR A 108 22.439 50.097 17.351 1.00 14.29 7872 CA THR A 108 22.316 48.792 18.020 1.00 14.34 6 873 C THR A 10823.305 48.617 19.154 1.00 16.18 6 874 O THR A 108 22.945 48.095 20.2241.00 14.57 8 875 CB THR A 108 22.508 47.669 16.969 1.00 16.38 6 876 OG1THR A 108 21.473 47.841 16.005 1.00 18.39 8 877 CG2 THR A 108 22.38646.276 17.600 1.00 20.41 6 878 N THR A 109 24.581 49.043 18.959 1.0012.36 7 879 CA THR A 109 25.556 48.897 20.029 1.00 13.35 6 880 C THR A109 25.149 49.732 21.248 1.00 12.11 6 881 O THR A 109 25.318 49.28222.382 1.00 12.78 8 882 CB THR A 109 26.960 49.404 19.545 1.00 13.85 6883 OG1 THR A 109 27.201 49.021 18.155 1.00 14.22 8 884 CG2 THR A 10928.048 48.783 20.429 1.00 15.14 6 885 N PHE A 110 24.673 50.945 20.9821.00 12.96 7 886 CA PHE A 110 24.247 51.800 22.126 1.00 12.43 6 887 CPHE A 110 23.058 51.137 22.830 1.00 13.48 6 888 O PHE A 110 23.06151.036 24.060 1.00 12.36 8 889 CB PHE A 110 23.823 53.160 21.525 1.0014.28 6 890 CG PHE A 110 23.320 54.128 22.611 1.00 15.08 6 891 CD1 PHE A110 24.190 54.941 23.252 1.00 13.29 6 892 CD2 PHE A 110 21.975 54.20222.913 1.00 14.29 6 893 CE1 PHE A 110 23.764 55.850 24.247 1.00 13.20 6894 CE2 PHE A 110 21.487 55.055 23.876 1.00 12.89 6 895 CZ PHE A 11022.377 55.898 24.558 1.00 13.20 6 896 N ASP A 111 22.056 50.645 22.0651.00 13.15 7 897 CA ASP A 111 20.916 49.993 22.755 1.00 12.63 6 898 CASP A 111 21.337 48.770 23.517 1.00 14.08 6 899 O ASP A 111 20.91748.606 24.698 1.00 14.41 8 900 CB ASP A 111 19.966 49.513 21.610 1.0013.40 6 901 CG ASP A 111 19.224 50.603 20.937 1.00 18.96 6 902 OD1 ASP A111 19.343 51.768 21.305 1.00 17.72 8 903 OD2 ASP A 111 18.498 50.29119.945 1.00 18.78 8 904 N THR A 112 22.284 48.006 22.997 1.00 13.38 7905 CA THR A 112 22.756 46.828 23.718 1.00 14.87 6 906 C THR A 11223.450 47.184 25.017 1.00 14.48 6 907 O THR A 112 23.224 46.583 26.0691.00 15.04 8 908 CB THR A 112 23.680 45.966 22.829 1.00 15.99 6 909 OG1THR A 112 22.844 45.644 21.711 1.00 16.67 8 910 CG2 THR A 112 24.00644.662 23.576 1.00 18.86 6 911 N LEU A 113 24.321 48.221 24.968 1.0011.85 7 912 CA LEU A 113 24.982 48.631 26.219 1.00 12.44 6 913 C LEU A113 23.992 49.138 27.242 1.00 12.26 6 914 O LEU A 113 24.057 48.79328.403 1.00 12.86 8 915 CB LEU A 113 25.988 49.772 25.811 1.00 10.14 6916 CG LEU A 113 26.404 50.629 27.037 1.00 13.26 6 917 CD1 LEU A 11327.184 49.772 28.040 1.00 13.59 6 918 CD2 LEU A 113 27.295 51.825 26.6641.00 12.75 6 919 N VAL A 114 23.020 49.971 26.823 1.00 11.82 7 920 CAVAL A 114 22.073 50.545 27.762 1.00 12.84 6 921 C VAL A 114 21.21549.449 28.384 1.00 13.48 6 922 O VAL A 114 20.973 49.402 29.577 1.0013.54 8 923 CB VAL A 114 21.264 51.680 27.090 1.00 13.71 6 924 CG1 VAL A114 20.144 52.091 28.032 1.00 18.18 6 925 CG2 VAL A 114 22.209 52.88526.815 1.00 15.06 6 926 N ASN A 115 20.760 48.534 27.512 1.00 13.50 7927 CA ASN A 115 19.912 47.430 28.013 1.00 11.60 6 928 C ASN A 11520.678 46.553 28.961 1.00 12.99 6 929 O ASN A 115 20.121 46.160 29.9871.00 15.11 8 930 CB ASN A 115 19.372 46.637 26.820 1.00 15.99 6 931 CGASN A 115 18.200 47.261 26.118 1.00 22.41 6 932 OD1 ASN A 115 18.06147.131 24.868 1.00 26.38 8 933 ND2 ASN A 115 17.304 47.937 26.823 1.0022.30 7 934 N ASP A 116 21.940 46.229 28.669 1.00 12.94 7 935 CA ASP A116 22.731 45.386 29.561 1.00 12.20 6 936 C ASP A 116 23.087 46.14430.835 1.00 12.69 6 937 O ASP A 116 23.070 45.584 31.933 1.00 12.40 8938 CB ASP A 116 23.989 44.814 28.887 1.00 13.19 6 939 CG ASP A 11623.648 43.698 27.896 1.00 19.33 6 940 OD1 ASP A 116 22.461 43.487 27.5821.00 23.80 8 941 OD2 ASP A 116 24.583 42.967 27.460 1.00 22.90 8 942 NALA A 117 23.342 47.453 30.753 1.00 12.25 7 943 CA ALA A 117 23.56148.208 32.005 1.00 12.13 6 944 C ALA A 117 22.314 48.146 32.878 1.0010.66 6 945 O ALA A 117 22.425 47.887 34.083 1.00 12.92 8 946 CB ALA A117 23.877 49.692 31.625 1.00 13.05 6 947 N HIS A 118 21.149 48.40332.291 1.00 12.02 7 948 CA HIS A 118 19.948 48.334 33.131 1.00 10.66 6949 C HIS A 118 19.727 46.929 33.683 1.00 12.65 6 950 O HIS A 118 19.26746.870 34.838 1.00 14.87 8 951 CB HIS A 118 18.714 48.622 32.200 1.0010.79 6 952 CG HIS A 118 18.691 50.088 31.789 1.00 11.37 6 953 ND1 HIS A118 17.881 50.557 30.773 1.00 14.86 7 954 CD2 HIS A 118 19.340 51.15732.359 1.00 13.69 6 955 CE1 HIS A 118 18.020 51.897 30.708 1.00 15.91 6956 NE2 HIS A 118 18.912 52.260 31.644 1.00 11.99 7 957 N GLN A 11920.028 45.871 32.935 1.00 11.93 7 958 CA GLN A 119 19.843 44.545 33.5921.00 12.22 6 959 C GLN A 119 20.770 44.412 34.781 1.00 15.02 6 960 O GLNA 119 20.519 43.615 35.694 1.00 15.33 8 961 CB GLN A 119 20.340 43.44532.620 1.00 16.20 6 962 CG GLN A 119 19.327 43.169 31.521 1.00 17.09 6963 CD GLN A 119 20.028 41.969 30.765 1.00 21.33 6 964 OE1 GLN A 11920.575 41.051 31.363 1.00 29.71 8 965 NE2 GLN A 119 19.985 42.085 29.5221.00 20.93 7 966 N ASN A 120 21.939 45.127 34.806 1.00 15.33 7 967 CAASN A 120 22.853 45.072 35.932 1.00 16.39 6 968 C ASN A 120 22.54146.148 36.970 1.00 14.25 6 969 O ASN A 120 23.358 46.337 37.876 1.0015.65 8 970 CB ASN A 120 24.337 45.189 35.481 1.00 12.26 6 971 CG ASN A120 24.753 43.901 34.799 1.00 20.80 6 972 OD1 ASN A 120 24.778 43.80533.576 1.00 23.34 8 973 ND2 ASN A 120 25.076 42.912 35.627 1.00 18.29 7974 N GLY A 121 21.398 46.801 36.951 1.00 13.35 7 975 CA GLY A 12120.994 47.834 37.885 1.00 16.91 6 976 C GLY A 121 21.840 49.129 37.7721.00 13.99 6 977 O GLY A 121 21.866 49.890 38.747 1.00 15.35 8 978 N ILEA 122 22.262 49.397 36.527 1.00 12.67 7 979 CA ILE A 122 23.128 50.56936.322 1.00 13.01 6 980 C ILE A 122 22.464 51.454 35.289 1.00 13.96 6981 O ILE A 122 22.075 50.945 34.227 1.00 12.86 8 982 CB ILE A 12224.556 50.129 35.886 1.00 12.06 6 983 CG1 ILE A 122 25.320 49.424 37.0401.00 15.35 6 984 CG2 ILE A 122 25.415 51.348 35.506 1.00 13.36 6 985 CD1ILE A 122 26.569 48.709 36.465 1.00 15.31 6 986 N LYS A 123 22.34452.752 35.609 1.00 11.45 7 987 CA LYS A 123 21.767 53.718 34.652 1.0011.74 6 988 C LYS A 123 22.865 54.362 33.786 1.00 11.74 6 989 O LYS A123 24.052 54.129 34.057 1.00 11.17 8 990 CB LYS A 123 21.051 54.81135.457 1.00 11.34 6 991 CG LYS A 123 19.832 54.205 36.163 1.00 12.23 6992 CD LYS A 123 18.994 55.310 36.815 1.00 16.30 6 993 CE LYS A 12319.601 56.014 38.025 1.00 21.38 6 994 NZ LYS A 123 20.133 55.054 39.0001.00 25.83 7 995 N VAL A 124 22.372 54.936 32.656 1.00 9.54 7 996 CA VALA 124 23.343 55.533 31.740 1.00 9.53 6 997 C VAL A 124 22.856 56.95431.460 1.00 12.31 6 998 O VAL A 124 21.723 57.168 30.990 1.00 12.23 8999 CB VAL A 124 23.372 54.748 30.408 1.00 12.71 6 1000 CG1 VAL A 12424.327 55.480 29.398 1.00 12.93 6 1001 CG2 VAL A 124 23.875 53.31330.661 1.00 11.85 6 1002 N ILE A 125 23.726 57.937 31.756 1.00 10.85 71003 CA ILE A 125 23.419 59.311 31.352 1.00 10.22 6 1004 C ILE A 12524.430 59.676 30.232 1.00 11.59 6 1005 O ILE A 125 25.549 59.113 30.2201.00 12.11 8 1006 CB ILE A 125 23.403 60.385 32.474 1.00 10.25 6 1007CG1 ILE A 125 24.811 60.531 33.089 1.00 13.12 6 1008 CG2 ILE A 12522.304 60.035 33.484 1.00 9.99 6 1009 CD1 ILE A 125 24.770 61.746 34.0841.00 17.03 6 1010 N VAL A 126 23.971 60.450 29.252 1.00 9.62 7 1011 CAVAL A 126 24.864 60.725 28.102 1.00 10.33 6 1012 C VAL A 126 25.24762.207 28.081 1.00 12.61 6 1013 O VAL A 126 24.413 63.080 28.254 1.0011.41 8 1014 CB VAL A 126 24.039 60.356 26.823 1.00 11.44 6 1015 CG1 VALA 126 24.892 60.704 25.575 1.00 12.92 6 1016 CG2 VAL A 126 23.704 58.88326.856 1.00 11.52 6 1017 N ASP A 127 26.535 62.445 27.771 1.00 8.46 71018 CA ASP A 127 27.011 63.870 27.661 1.00 9.67 6 1019 C ASP A 12726.509 64.374 26.283 1.00 10.71 6 1020 O ASP A 127 26.837 63.710 25.2791.00 11.36 8 1021 CB ASP A 127 28.552 63.719 27.694 1.00 9.91 6 1022 CGASP A 127 29.305 64.951 28.135 1.00 11.94 6 1023 OD1 ASP A 127 28.82266.041 27.747 1.00 11.17 8 1024 OD2 ASP A 127 30.335 64.880 28.865 1.0010.63 8 1025 N PHE A 128 25.802 65.484 26.325 1.00 8.41 7 1026 CA PHE A128 25.134 65.952 25.077 1.00 9.40 6 1027 C PHE A 128 25.609 67.39424.887 1.00 9.48 6 1028 O PHE A 128 25.752 68.163 25.858 1.00 10.67 81029 CB PHE A 128 23.609 66.006 25.437 1.00 9.59 6 1030 CG PHE A 12822.760 66.405 24.223 1.00 8.93 6 1031 CD1 PHE A 128 22.719 65.597 23.1041.00 12.26 6 1032 CD2 PHE A 128 22.095 67.627 24.315 1.00 10.12 6 1033CE1 PHE A 128 21.907 66.014 22.027 1.00 12.04 6 1034 CE2 PHE A 12821.325 67.993 23.183 1.00 10.05 6 1035 CZ PHE A 128 21.229 67.218 22.0701.00 10.20 6 1036 N VAL A 129 25.985 67.736 23.647 1.00 8.13 7 1037 CAVAL A 129 26.851 68.932 23.398 1.00 9.78 6 1038 C VAL A 129 26.17169.845 22.412 1.00 9.18 6 1039 O VAL A 129 26.494 70.026 21.210 1.0010.74 8 1040 CB VAL A 129 28.178 68.381 22.804 1.00 11.28 6 1041 CG1 VALA 129 29.206 69.539 22.719 1.00 12.02 6 1042 CG2 VAL A 129 28.829 67.24623.590 1.00 10.62 6 1043 N PRO A 130 25.165 70.638 22.855 1.00 10.64 71044 CA PRO A 130 24.341 71.474 21.986 1.00 10.69 6 1045 C PRO A 13024.946 72.802 21.588 1.00 11.36 6 1046 O PRO A 130 24.336 73.565 20.8141.00 11.49 8 1047 CB PRO A 130 22.983 71.673 22.735 1.00 10.77 6 1048 CGPRO A 130 23.480 71.602 24.189 1.00 12.02 6 1049 CD PRO A 130 24.59370.514 24.205 1.00 11.44 6 1050 N ASN A 131 26.107 73.181 22.144 1.009.48 7 1051 CA ASN A 131 26.687 74.481 21.859 1.00 10.43 6 1052 C ASN A131 27.244 74.637 20.438 1.00 11.66 6 1053 O ASN A 131 27.256 75.72419.881 1.00 11.65 8 1054 CB ASN A 131 27.756 74.902 22.877 1.00 10.94 61055 CG ASN A 131 28.233 76.316 22.592 1.00 10.72 6 1056 OD1 ASN A 13127.396 77.205 22.783 1.00 10.02 8 1057 ND2 ASN A 131 29.516 76.44722.224 1.00 10.08 7 1058 N HIS A 132 27.676 73.513 19.855 1.00 10.71 71059 CA HIS A 132 28.476 73.726 18.632 1.00 9.32 6 1060 C HIS A 13228.552 72.441 17.845 1.00 9.83 6 1061 O HIS A 132 28.256 71.362 18.3611.00 12.46 8 1062 CB HIS A 132 29.896 74.227 19.005 1.00 11.52 6 1063 CGHIS A 132 30.560 73.394 20.080 1.00 10.70 6 1064 ND1 HIS A 132 30.61673.869 21.372 1.00 11.00 7 1065 CD2 HIS A 132 31.084 72.152 20.032 1.009.99 6 1066 CE1 HIS A 132 31.189 72.945 22.154 1.00 12.39 6 1067 NE2 HISA 132 31.445 71.929 21.368 1.00 10.00 7 1068 N SER A 133 28.999 72.60816.584 1.00 10.23 7 1069 CA SER A 133 29.365 71.428 15.787 1.00 10.30 61070 C SER A 133 30.876 71.239 15.861 1.00 11.64 6 1071 O SER A 13331.319 70.652 16.863 1.00 11.94 8 1072 CB SER A 133 28.807 71.514 14.3441.00 10.65 6 1073 OG SER A 133 29.342 72.683 13.700 1.00 11.57 8 1074 NTHR A 134 31.611 71.535 14.805 1.00 11.30 7 1075 CA THR A 134 33.03471.082 14.740 1.00 10.51 6 1076 C THR A 134 33.959 72.251 14.424 1.008.56 6 1077 O THR A 134 33.553 73.376 14.121 1.00 10.40 8 1078 CB THR A134 33.119 70.005 13.630 1.00 9.65 6 1079 OG1 THR A 134 32.559 70.59612.429 1.00 11.51 8 1080 CG2 THR A 134 32.295 68.752 13.956 1.00 11.00 61081 N PRO A 135 35.256 71.959 14.489 1.00 10.51 7 1082 CA PRO A 13536.320 72.955 14.289 1.00 12.33 6 1083 C PRO A 135 36.264 73.606 12.8991.00 12.27 6 1084 O PRO A 135 36.014 72.968 11.868 1.00 13.19 8 1085 CBPRO A 135 37.627 72.145 14.405 1.00 11.11 6 1086 CG PRO A 135 37.24171.129 15.486 1.00 11.56 6 1087 CD PRO A 135 35.809 70.746 15.111 1.0011.98 6 1088 N PHE A 136 36.500 74.966 12.885 1.00 10.88 7 1089 CA PHE A136 36.606 75.628 11.597 1.00 11.37 6 1090 C PHE A 136 37.536 76.83011.718 1.00 11.99 6 1091 O PHE A 136 37.856 77.248 12.827 1.00 12.95 81092 CB PHE A 136 35.176 76.074 11.125 1.00 13.36 6 1093 CG PHE A 13634.690 77.341 11.793 1.00 15.31 6 1094 CD1 PHE A 136 34.201 77.31113.100 1.00 12.18 6 1095 CD2 PHE A 136 34.801 78.565 11.134 1.00 13.24 61096 CE1 PHE A 136 33.813 78.477 13.738 1.00 13.44 6 1097 CE2 PHE A 13634.451 79.741 11.779 1.00 12.17 6 1098 CZ PHE A 136 33.903 79.708 13.0871.00 15.41 6 1099 N LYS A 137 38.037 77.258 10.547 1.00 11.70 7 1100 CALYS A 137 38.710 78.567 10.479 1.00 10.33 6 1101 C LYS A 137 37.85979.484 9.618 1.00 13.10 6 1102 O LYS A 137 37.493 79.111 8.490 1.0012.91 8 1103 CB LYS A 137 40.060 78.360 9.724 1.00 17.76 6 1104 CG LYS A137 41.153 77.554 10.411 1.00 19.69 6 1105 CD LYS A 137 41.439 78.04911.810 1.00 22.72 6 1106 CE LYS A 137 42.145 79.366 12.006 1.00 31.41 61107 NZ LYS A 137 43.212 79.771 11.035 1.00 25.39 7 1108 N ALA A 13837.657 80.688 10.158 1.00 12.09 7 1109 CA ALA A 138 36.683 81.510 9.3751.00 12.57 6 1110 C ALA A 138 37.267 81.873 8.017 1.00 14.60 6 1111 OALA A 138 36.469 82.176 7.094 1.00 14.01 8 1112 CB ALA A 138 36.41082.806 10.148 1.00 15.45 6 1113 N ASN A 139 38.597 81.986 7.900 1.0013.25 7 1114 CA ASN A 139 39.165 82.359 6.608 1.00 14.41 6 1115 C ASN A139 39.444 81.212 5.682 1.00 14.25 6 1116 O ASN A 139 40.047 81.3494.562 1.00 14.82 8 1117 CB ASN A 139 40.443 83.188 6.852 1.00 16.78 61118 CG ASN A 139 41.666 82.292 7.083 1.00 22.27 6 1119 OD1 ASN A 13941.484 81.167 7.486 1.00 25.66 8 1120 ND2 ASN A 139 42.853 82.762 6.7731.00 21.53 7 1121 N ASP A 140 39.150 79.955 6.052 1.00 14.76 7 1122 CAASP A 140 39.433 78.835 5.203 1.00 13.60 6 1123 C ASP A 140 38.47077.674 5.337 1.00 16.09 6 1124 O ASP A 140 38.607 76.905 6.339 1.0013.95 8 1125 CB ASP A 140 40.885 78.382 5.557 1.00 12.14 6 1126 CG ASP A140 41.331 77.260 4.643 1.00 16.87 6 1127 OD1 ASP A 140 40.616 76.7053.810 1.00 17.82 8 1128 OD2 ASP A 140 42.569 76.954 4.814 1.00 25.09 81129 N SER A 141 37.529 77.555 4.414 1.00 15.21 7 1130 CA SER A 14136.508 76.520 4.501 1.00 16.63 6 1131 C SER A 141 37.048 75.092 4.2851.00 17.44 6 1132 O SER A 141 36.349 74.129 4.607 1.00 18.28 8 1133 CBSER A 141 35.372 76.746 3.493 1.00 19.52 6 1134 OG SER A 141 35.86776.579 2.144 1.00 16.38 8 1135 N THR A 142 38.302 74.958 3.839 1.0014.08 7 1136 CA THR A 142 38.889 73.615 3.649 1.00 15.63 6 1137 C THR A142 39.445 73.036 4.933 1.00 16.91 6 1138 O THR A 142 39.798 71.8404.961 1.00 15.67 8 1139 CB THR A 142 40.105 73.658 2.622 1.00 16.69 61140 OG1 THR A 142 41.261 74.288 3.211 1.00 18.35 8 1141 CG2 THR A 14239.653 74.352 1.368 1.00 25.03 6 1142 N PHE A 143 39.533 73.874 6.0071.00 15.48 7 1143 CA PHE A 143 40.027 73.314 7.285 1.00 12.99 6 1144 CPHE A 143 38.953 72.384 7.908 1.00 14.57 6 1145 O PHE A 143 37.80772.837 8.026 1.00 12.49 8 1146 CB PHE A 143 40.412 74.481 8.238 1.0014.72 6 1147 CG PHE A 143 40.905 73.939 9.546 1.00 13.33 6 1148 CD1 PHEA 143 42.192 73.454 9.669 1.00 14.66 6 1149 CD2 PHE A 143 40.054 73.90810.679 1.00 10.60 6 1150 CE1 PHE A 143 42.677 72.946 10.878 1.00 14.87 61151 CE2 PHE A 143 40.556 73.381 11.849 1.00 12.09 6 1152 CZ PHE A 14341.842 72.912 11.975 1.00 16.30 6 1153 N ALA A 144 39.342 71.174 8.2641.00 14.83 7 1154 CA ALA A 144 38.380 70.250 8.884 1.00 14.49 6 1155 CALA A 144 37.165 70.136 7.976 1.00 14.94 6 1156 O ALA A 144 37.36969.878 6.784 1.00 13.97 8 1157 CB ALA A 144 37.990 70.683 10.323 1.0012.28 6 1158 N GLU A 145 35.942 70.135 8.506 1.00 11.43 7 1159 CA GLU A145 34.744 70.061 7.645 1.00 10.19 6 1160 C GLU A 145 34.063 71.3867.520 1.00 10.66 6 1161 O GLU A 145 32.824 71.513 7.266 1.00 11.84 81162 CB GLU A 145 33.771 68.943 8.180 1.00 11.91 6 1163 CG GLU A 14534.408 67.577 8.042 1.00 11.68 6 1164 CD GLU A 145 33.591 66.467 8.6971.00 15.77 6 1165 OE1 GLU A 145 32.530 66.660 9.208 1.00 20.95 8 1166OE2 GLU A 145 34.122 65.351 8.743 1.00 21.22 8 1167 N GLY A 146 34.67772.533 7.898 1.00 12.55 7 1168 CA GLY A 146 34.021 73.826 7.783 1.0012.03 6 1169 C GLY A 146 32.799 73.976 8.739 1.00 15.18 6 1170 O GLY A146 32.025 74.880 8.511 1.00 13.95 8 1171 N GLY A 147 32.774 73.1579.790 1.00 12.57 7 1172 CA GLY A 147 31.639 73.265 10.703 1.00 12.28 61173 C GLY A 147 30.439 72.415 10.267 1.00 14.09 6 1174 O GLY A 14729.372 72.644 10.903 1.00 11.87 8 1175 N ALA A 148 30.552 71.583 9.2581.00 11.40 7 1176 CA ALA A 148 29.343 70.942 8.707 1.00 13.48 6 1177 CALA A 148 28.495 70.132 9.729 1.00 11.58 6 1178 O ALA A 148 29.02569.390 10.557 1.00 12.14 8 1179 CB ALA A 148 29.861 69.927 7.660 1.0014.52 6 1180 N LEU A 149 27.188 70.305 9.543 1.00 12.19 7 1181 CA LEU A149 26.192 69.594 10.365 1.00 10.39 6 1182 C LEU A 149 25.298 68.7989.407 1.00 10.91 6 1183 O LEU A 149 24.907 69.311 8.313 1.00 14.52 81184 CB LEU A 149 25.345 70.684 11.028 1.00 10.56 6 1185 CG LEU A 14924.344 70.222 12.098 1.00 14.34 6 1186 CD1 LEU A 149 25.067 69.61813.294 1.00 16.21 6 1187 CD2 LEU A 149 23.436 71.409 12.447 1.00 15.60 61188 N TYR A 150 25.047 67.560 9.836 1.00 12.69 7 1189 CA TYR A 15024.178 66.675 9.057 1.00 11.91 6 1190 C TYR A 150 23.007 66.234 9.9571.00 13.54 6 1191 O TYR A 150 23.116 66.203 11.188 1.00 12.53 8 1192 CBTYR A 150 24.945 65.392 8.671 1.00 12.62 6 1193 CG TYR A 150 26.10465.699 7.694 1.00 10.80 6 1194 CD1 TYR A 150 27.275 66.240 8.185 1.0013.28 6 1195 CD2 TYR A 150 25.983 65.330 6.359 1.00 14.10 6 1196 CE1 TYRA 150 28.295 66.545 7.273 1.00 14.81 6 1197 CE2 TYR A 150 27.004 65.6095.479 1.00 17.28 6 1198 CZ TYR A 150 28.139 66.206 5.959 1.00 17.89 61199 OH TYR A 150 29.227 66.444 5.082 1.00 18.31 8 1200 N ASN A 15121.932 65.787 9.288 1.00 11.59 7 1201 CA ASN A 151 20.774 65.261 10.0481.00 13.13 6 1202 C ASN A 151 20.582 63.801 9.659 1.00 14.46 6 1203 OASN A 151 20.020 63.527 8.595 1.00 15.41 8 1204 CB ASN A 151 19.54266.068 9.633 1.00 12.78 6 1205 CG ASN A 151 18.280 65.607 10.386 1.0015.85 6 1206 OD1 ASN A 151 18.376 65.084 11.460 1.00 14.91 8 1207 ND2ASN A 151 17.115 65.851 9.790 1.00 23.13 7 1208 N ASN A 152 21.15362.881 10.455 1.00 11.88 7 1209 CA ASN A 152 21.160 61.460 10.056 1.0012.91 6 1210 C ASN A 152 21.628 61.265 8.619 1.00 17.10 6 1211 O ASN A152 21.059 60.495 7.804 1.00 18.15 8 1212 CB ASN A 152 19.763 60.89410.305 1.00 15.18 6 1213 CG ASN A 152 19.772 59.363 10.289 1.00 28.25 61214 OD1 ASN A 152 20.803 58.741 10.579 1.00 25.62 8 1215 ND2 ASN A 15218.647 58.722 9.925 1.00 26.09 7 1216 N GLY A 153 22.797 61.857 8.3441.00 11.86 7 1217 CA GLY A 153 23.494 61.698 7.061 1.00 15.63 6 1218 CGLY A 153 23.096 62.727 6.007 1.00 17.70 6 1219 O GLY A 153 23.81962.836 4.994 1.00 16.41 8 1220 N THR A 154 21.975 63.414 6.209 1.0013.77 7 1221 CA THR A 154 21.535 64.406 5.220 1.00 14.28 6 1222 C THR A154 22.181 65.781 5.538 1.00 14.24 6 1223 O THR A 154 22.048 66.2646.650 1.00 15.31 8 1224 CB THR A 154 20.008 64.592 5.212 1.00 21.10 61225 OG1 THR A 154 19.488 63.334 4.709 1.00 20.66 8 1226 CG2 THR A 15419.569 65.711 4.260 1.00 21.99 6 1227 N TYR A 155 22.977 66.280 4.5661.00 14.57 7 1228 CA TYR A 155 23.613 67.573 4.928 1.00 15.65 6 1229 CTYR A 155 22.652 68.698 5.184 1.00 17.55 6 1230 O TYR A 155 21.63968.912 4.487 1.00 16.44 8 1231 CB TYR A 155 24.440 67.984 3.678 1.0016.08 6 1232 CG TYR A 155 25.238 69.243 3.820 1.00 16.71 6 1233 CD1 TYRA 155 26.324 69.277 4.693 1.00 16.20 6 1234 CD2 TYR A 155 24.989 70.3813.075 1.00 16.54 6 1235 CE1 TYR A 155 27.139 70.407 4.789 1.00 16.44 61236 CE2 TYR A 155 25.773 71.530 3.162 1.00 14.17 6 1237 CZ TYR A 15526.843 71.515 4.015 1.00 16.83 6 1238 OH TYR A 155 27.673 72.601 4.1421.00 15.80 8 1239 N MET A 156 22.895 69.456 6.272 1.00 12.36 7 1240 CAMET A 156 22.120 70.658 6.595 1.00 12.72 6 1241 C MET A 156 22.87771.939 6.202 1.00 14.70 6 1242 O MET A 156 22.290 72.876 5.628 1.0014.86 8 1243 CB MET A 156 21.886 70.683 8.141 1.00 14.72 6 1244 CG MET A156 21.045 69.510 8.543 1.00 13.16 6 1245 SD MET A 156 20.812 69.39110.354 1.00 16.44 16 1246 CE MET A 156 19.828 70.788 10.735 1.00 16.14 61247 N GLY A 157 24.138 72.003 6.634 1.00 15.28 7 1248 CA GLY A 15724.888 73.257 6.260 1.00 12.22 6 1249 C GLY A 157 26.169 73.337 7.0611.00 15.29 6 1250 O GLY A 157 26.402 72.513 7.965 1.00 13.96 8 1251 NASN A 158 26.981 74.369 6.736 1.00 13.19 7 1252 CA ASN A 158 28.20574.586 7.485 1.00 12.06 6 1253 C ASN A 158 28.353 76.085 7.759 1.00 8.806 1254 O ASN A 158 27.377 76.850 7.583 1.00 11.73 8 1255 CB ASN A 15829.438 73.957 6.787 1.00 12.79 6 1256 CG ASN A 158 29.783 74.647 5.4571.00 16.08 6 1257 OD1 ASN A 158 29.311 75.727 5.160 1.00 12.69 8 1258ND2 ASN A 158 30.650 74.060 4.603 1.00 20.88 7 1259 N TYR A 159 29.55976.484 8.260 1.00 10.67 7 1260 CA TYR A 159 29.714 77.924 8.640 1.0011.67 6 1261 C TYR A 159 29.665 78.827 7.432 1.00 12.87 6 1262 O TYR A159 29.444 80.029 7.605 1.00 12.70 8 1263 CB TYR A 159 31.055 78.0729.434 1.00 11.86 6 1264 CG TYR A 159 31.171 79.475 10.063 1.00 11.61 61265 CD1 TYR A 159 30.414 79.868 11.149 1.00 14.86 6 1266 CD2 TYR A 15931.962 80.402 9.380 1.00 13.87 6 1267 CE1 TYR A 159 30.576 81.181 11.6001.00 15.19 6 1268 CE2 TYR A 159 32.069 81.716 9.811 1.00 19.88 6 1269 CZTYR A 159 31.387 82.088 10.926 1.00 16.15 6 1270 OH TYR A 159 31.37783.383 11.432 1.00 16.24 8 1271 N PHE A 160 29.904 78.307 6.253 1.0013.52 7 1272 CA PHE A 160 30.073 79.126 5.029 1.00 12.84 6 1273 C PHE A160 28.855 79.182 4.153 1.00 12.34 6 1274 O PHE A 160 28.803 80.1013.300 1.00 14.63 8 1275 CB PHE A 160 31.228 78.421 4.234 1.00 12.99 61276 CG PHE A 160 32.504 78.508 5.080 1.00 14.21 6 1277 CD1 PHE A 16033.310 79.662 4.935 1.00 12.64 6 1278 CD2 PHE A 160 32.804 77.488 5.9651.00 12.84 6 1279 CE1 PHE A 160 34.466 79.772 5.737 1.00 14.91 6 1280CE2 PHE A 160 33.940 77.621 6.761 1.00 14.27 6 1281 CZ PHE A 160 34.76978.740 6.653 1.00 13.93 6 1282 N ASP A 161 27.917 78.220 4.232 1.0014.16 7 1283 CA ASP A 161 26.731 78.329 3.371 1.00 14.46 6 1284 C ASP A161 25.486 78.622 4.217 1.00 14.25 6 1285 O ASP A 161 24.375 78.2153.808 1.00 15.23 8 1286 CB ASP A 161 26.557 77.031 2.565 1.00 12.66 61287 CG ASP A 161 26.500 75.766 3.373 1.00 15.72 6 1288 OD1 ASP A 16126.191 75.896 4.579 1.00 13.04 8 1289 OD2 ASP A 161 26.767 74.716 2.7661.00 20.26 8 1290 N ASP A 162 25.656 79.460 5.227 1.00 13.84 7 1291 CAASP A 162 24.557 79.667 6.196 1.00 14.60 6 1292 C ASP A 162 23.78780.939 5.979 1.00 16.54 6 1293 O ASP A 162 22.840 81.252 6.726 1.0018.25 8 1294 CB ASP A 162 25.253 79.785 7.584 1.00 12.11 6 1295 CG ASP A162 24.264 79.524 8.717 1.00 13.12 6 1296 OD1 ASP A 162 23.408 78.6248.551 1.00 12.76 8 1297 OD2 ASP A 162 24.417 80.201 9.775 1.00 12.76 81298 N ALA A 163 24.109 81.725 4.949 1.00 16.09 7 1299 CA ALA A 16323.428 83.019 4.792 1.00 16.11 6 1300 C ALA A 163 21.914 82.901 4.8481.00 17.25 6 1301 O ALA A 163 21.341 83.825 5.467 1.00 24.30 8 1302 CBALA A 163 23.828 83.609 3.414 1.00 19.57 6 1303 N THR A 164 21.31781.987 4.145 1.00 19.25 7 1304 CA THR A 164 19.845 81.973 4.121 1.0024.11 6 1305 C THR A 164 19.237 81.014 5.149 1.00 25.86 6 1306 O THR A164 18.055 80.605 5.002 1.00 25.38 8 1307 CB THR A 164 19.384 81.5022.723 1.00 21.33 6 1308 OG1 THR A 164 19.834 80.146 2.496 1.00 29.22 81309 CG2 THR A 164 20.062 82.359 1.658 1.00 32.67 6 1310 N LYS A 16520.086 80.431 6.008 1.00 19.16 7 1311 CA LYS A 165 19.577 79.430 6.9291.00 16.62 6 1312 C LYS A 165 19.714 79.888 8.391 1.00 18.03 6 1313 OLYS A 165 18.735 79.767 9.173 1.00 17.25 8 1314 CB LYS A 165 20.42378.140 6.826 1.00 13.80 6 1315 CG LYS A 165 20.215 77.497 5.423 1.0021.49 6 1316 CD LYS A 165 20.913 76.186 5.334 1.00 30.47 6 1317 CE LYS A165 22.394 76.297 5.245 1.00 26.09 6 1318 NZ LYS A 165 23.067 75.3084.349 1.00 18.44 7 1319 N GLY A 166 20.839 80.499 8.700 1.00 14.27 71320 CA GLY A 166 21.048 81.024 10.082 1.00 14.43 6 1321 C GLY A 16621.103 79.863 11.109 1.00 14.80 6 1322 O GLY A 166 20.730 80.096 12.2871.00 14.92 8 1323 N TYR A 167 21.732 78.765 10.734 1.00 12.78 7 1324 CATYR A 167 21.882 77.692 11.732 1.00 12.54 6 1325 C TYR A 167 22.99178.009 12.739 1.00 12.62 6 1326 O TYR A 167 23.085 77.349 13.776 1.0011.78 8 1327 CB TYR A 167 22.226 76.374 11.022 1.00 10.92 6 1328 CG TYRA 167 21.127 75.836 10.103 1.00 14.63 6 1329 CD1 TYR A 167 19.810 76.23210.291 1.00 13.59 6 1330 CD2 TYR A 167 21.490 74.921 9.121 1.00 15.06 61331 CE1 TYR A 167 18.836 75.722 9.421 1.00 13.53 6 1332 CE2 TYR A 16720.503 74.385 8.254 1.00 12.93 6 1333 CZ TYR A 167 19.211 74.809 8.4691.00 15.10 6 1334 OH TYR A 167 18.235 74.289 7.594 1.00 18.52 8 1335 NPHE A 168 23.963 78.870 12.342 1.00 11.36 7 1336 CA PHE A 168 25.07279.208 13.244 1.00 11.20 6 1337 C PHE A 168 25.097 80.677 13.551 1.0012.02 6 1338 O PHE A 168 24.515 81.539 12.854 1.00 11.21 8 1339 CB PHE A168 26.432 78.934 12.493 1.00 13.41 6 1340 CG PHE A 168 26.552 77.45912.174 1.00 11.52 6 1341 CD1 PHE A 168 27.044 76.583 13.130 1.00 10.63 61342 CD2 PHE A 168 26.171 77.007 10.899 1.00 13.81 6 1343 CE1 PHE A 16827.122 75.214 12.765 1.00 12.04 6 1344 CE2 PHE A 168 26.250 75.63910.574 1.00 12.05 6 1345 CZ PHE A 168 26.752 74.751 11.518 1.00 12.13 61346 N HIS A 169 25.665 81.067 14.709 1.00 11.43 7 1347 CA HIS A 16925.979 82.473 14.979 1.00 12.52 6 1348 C HIS A 169 27.266 82.836 14.1951.00 11.69 6 1349 O HIS A 169 28.109 82.035 13.921 1.00 11.66 8 1350 CBHIS A 169 26.361 82.658 16.482 1.00 11.57 6 1351 CG HIS A 169 25.15782.347 17.376 1.00 11.97 6 1352 ND1 HIS A 169 25.403 81.657 18.588 1.0011.36 7 1353 CD2 HIS A 169 23.838 82.604 17.274 1.00 11.55 6 1354 CE1HIS A 169 24.195 81.518 19.195 1.00 12.02 6 1355 NE2 HIS A 169 23.23382.111 18.427 1.00 10.80 7 1356 N HIS A 170 27.295 84.147 13.797 1.0011.77 7 1357 CA HIS A 170 28.474 84.629 13.015 1.00 12.20 6 1358 C HIS A170 29.029 85.872 13.672 1.00 14.93 6 1359 O HIS A 170 29.174 86.97413.053 1.00 16.92 8 1360 CB HIS A 170 28.083 84.949 11.533 1.00 13.28 61361 CG HIS A 170 27.535 83.698 10.888 1.00 12.02 6 1362 ND1 HIS A 17028.327 82.925 10.069 1.00 15.51 7 1363 CD2 HIS A 170 26.306 83.08810.915 1.00 13.12 6 1364 CE1 HIS A 170 27.639 81.863 9.689 1.00 16.69 61365 NE2 HIS A 170 26.409 81.953 10.156 1.00 13.32 7 1366 N ASN A 17129.387 85.778 14.962 1.00 12.58 7 1367 CA ASN A 171 29.735 86.967 15.7331.00 12.76 6 1368 C ASN A 171 31.201 87.040 16.147 1.00 13.34 6 1369 OASN A 171 31.554 87.947 16.949 1.00 17.31 8 1370 CB ASN A 171 28.91686.961 17.054 1.00 13.40 6 1371 CG ASN A 171 27.430 86.948 16.719 1.0017.12 6 1372 OD1 ASN A 171 26.595 86.168 17.252 1.00 16.54 8 1373 ND2ASN A 171 27.046 87.866 15.861 1.00 12.82 7 1374 N GLY A 172 32.01386.197 15.601 1.00 13.14 7 1375 CA GLY A 172 33.444 86.166 15.964 1.0015.42 6 1376 C GLY A 172 33.728 85.275 17.210 1.00 16.69 6 1377 O GLY A172 32.817 84.706 17.722 1.00 14.98 8 1378 N ASP A 173 34.993 85.18017.526 1.00 14.76 7 1379 CA ASP A 173 35.473 84.346 18.622 1.00 12.93 61380 C ASP A 173 35.292 84.996 19.976 1.00 12.76 6 1381 O ASP A 17335.410 86.248 20.131 1.00 11.79 8 1382 CB ASP A 173 36.980 84.152 18.3691.00 14.28 6 1383 CG ASP A 173 37.273 83.139 17.268 1.00 24.98 6 1384OD1 ASP A 173 36.398 82.387 16.822 1.00 17.11 8 1385 OD2 ASP A 17338.451 83.124 16.815 1.00 23.71 8 1386 N ILE A 174 35.073 84.127 20.9691.00 12.58 7 1387 CA ILE A 174 35.136 84.670 22.362 1.00 11.65 6 1388 CILE A 174 36.500 85.307 22.646 1.00 14.87 6 1389 O ILE A 174 37.50884.670 22.337 1.00 15.09 8 1390 CB ILE A 174 34.896 83.495 23.357 1.0013.27 6 1391 CG1 ILE A 174 33.431 83.005 23.177 1.00 10.95 6 1392 CG2ILE A 174 35.145 84.016 24.806 1.00 12.74 6 1393 CD1 ILE A 174 33.22081.690 24.000 1.00 11.77 6 1394 N SER A 175 36.441 86.493 23.260 1.0014.22 7 1395 CA SER A 175 37.710 87.093 23.770 1.00 16.89 6 1396 C SER A175 37.712 87.131 25.291 1.00 18.02 6 1397 O SER A 175 38.617 86.58725.938 1.00 19.20 8 1398 CB SER A 175 37.868 88.470 23.138 1.00 17.86 61399 OG SER A 175 39.049 89.044 23.724 1.00 24.28 8 1400 N ASN A 17636.650 87.662 25.854 1.00 14.39 7 1401 CA ASN A 176 36.515 87.678 27.3361.00 13.41 6 1402 C ASN A 176 35.511 86.561 27.678 1.00 12.76 6 1403 OASN A 176 34.286 86.760 27.482 1.00 13.43 8 1404 CB ASN A 176 35.89889.032 27.724 1.00 15.61 6 1405 CG ASN A 176 35.749 89.123 29.243 1.0017.91 6 1406 OD1 ASN A 176 35.963 88.166 29.982 1.00 15.18 8 1407 ND2ASN A 176 35.402 90.347 29.694 1.00 22.13 7 1408 N TRP A 177 36.08585.465 28.237 1.00 14.29 7 1409 CA TRP A 177 35.172 84.361 28.558 1.0013.39 6 1410 C TRP A 177 34.248 84.677 29.724 1.00 15.05 6 1411 O TRP A177 33.279 83.898 29.909 1.00 14.25 8 1412 CB TRP A 177 36.054 83.14528.953 1.00 16.12 6 1413 CG TRP A 177 36.712 82.559 27.721 1.00 14.43 61414 CD1 TRP A 177 37.745 83.101 26.998 1.00 16.58 6 1415 CD2 TRP A 17736.399 81.291 27.142 1.00 13.92 6 1416 NE1 TRP A 177 38.070 82.23525.940 1.00 18.57 7 1417 CE2 TRP A 177 37.234 81.131 26.014 1.00 18.68 61418 CE3 TRP A 177 35.437 80.298 27.392 1.00 17.34 6 1419 CZ2 TRP A 17737.148 80.031 25.169 1.00 14.28 6 1420 CZ3 TRP A 177 35.379 79.18226.574 1.00 17.20 6 1421 CH2 TRP A 177 36.253 79.045 25.441 1.00 18.00 61422 N ASP A 178 34.477 85.795 30.469 1.00 12.43 7 1423 CA ASP A 17833.507 86.126 31.517 1.00 11.08 6 1424 C ASP A 178 32.454 87.115 31.0531.00 12.88 6 1425 O ASP A 178 31.586 87.420 31.881 1.00 15.73 8 1426 CBASP A 178 34.243 86.717 32.739 1.00 17.78 6 1427 CG ASP A 178 35.20185.739 33.362 1.00 24.33 6 1428 OD1 ASP A 178 34.916 84.535 33.440 1.0018.07 8 1429 OD2 ASP A 178 36.317 86.155 33.777 1.00 24.77 8 1430 N ASPA 179 32.527 87.608 29.810 1.00 11.79 7 1431 CA ASP A 179 31.448 88.50229.357 1.00 11.42 6 1432 C ASP A 179 30.292 87.603 28.903 1.00 12.33 61433 O ASP A 179 30.537 86.725 28.067 1.00 12.08 8 1434 CB ASP A 17931.997 89.341 28.184 1.00 15.43 6 1435 CG ASP A 179 30.831 90.225 27.7631.00 18.80 6 1436 OD1 ASP A 179 30.462 91.232 28.431 1.00 20.56 8 1437OD2 ASP A 179 30.213 89.893 26.753 1.00 13.51 8 1438 N ARG A 180 29.11587.768 29.477 1.00 13.02 7 1439 CA ARG A 180 28.057 86.771 29.205 1.0011.54 6 1440 C ARG A 180 27.585 86.833 27.757 1.00 10.36 6 1441 O ARG A180 27.261 85.746 27.225 1.00 11.27 8 1442 CB ARG A 180 26.893 87.05130.172 1.00 13.31 6 1443 CG ARG A 180 27.286 86.796 31.654 1.00 12.49 61444 CD ARG A 180 27.797 85.340 31.899 1.00 10.75 6 1445 NE ARG A 18026.694 84.389 31.571 1.00 11.38 7 1446 CZ ARG A 180 26.896 83.305 30.8121.00 11.55 6 1447 NH1 ARG A 180 28.090 82.893 30.359 1.00 11.21 7 1448NH2 ARG A 180 25.769 82.597 30.589 1.00 13.64 7 1449 N TYR A 181 27.50887.990 27.113 1.00 10.51 7 1450 CA TYR A 181 27.104 87.980 25.688 1.0010.68 6 1451 C TYR A 181 28.195 87.277 24.870 1.00 11.14 6 1452 O TYR A181 27.826 86.403 24.044 1.00 10.66 8 1453 CB TYR A 181 26.915 89.44625.196 1.00 12.30 6 1454 CG TYR A 181 26.645 89.417 23.698 1.00 12.16 61455 CD1 TYR A 181 25.446 89.009 23.179 1.00 13.07 6 1456 CD2 TYR A 18127.712 89.736 22.837 1.00 15.09 6 1457 CE1 TYR A 181 25.242 88.93621.808 1.00 18.03 6 1458 CE2 TYR A 181 27.510 89.688 21.457 1.00 16.90 61459 CZ TYR A 181 26.275 89.265 20.988 1.00 19.76 6 1460 OH TYR A 18126.097 89.156 19.614 1.00 17.30 8 1461 N GLU A 182 29.473 87.528 25.0831.00 13.50 7 1462 CA GLU A 182 30.468 86.836 24.265 1.00 12.35 6 1463 CGLU A 182 30.442 85.311 24.504 1.00 10.45 6 1464 O GLU A 182 30.48284.533 23.582 1.00 11.45 8 1465 CB GLU A 182 31.939 87.266 24.571 1.0010.48 6 1466 CG GLU A 182 32.131 88.769 24.214 1.00 12.66 6 1467 CD GLUA 182 33.640 89.046 24.246 1.00 19.30 6 1468 OE1 GLU A 182 34.487 88.22923.958 1.00 15.48 8 1469 OE2 GLU A 182 34.009 90.199 24.690 1.00 30.95 81470 N ALA A 183 30.314 84.945 25.796 1.00 10.17 7 1471 CA ALA A 18330.436 83.521 26.110 1.00 11.02 6 1472 C ALA A 183 29.302 82.709 25.4711.00 11.67 6 1473 O ALA A 183 29.555 81.542 25.197 1.00 10.91 8 1474 CBALA A 183 30.290 83.352 27.664 1.00 11.34 6 1475 N GLN A 184 28.19683.381 25.172 1.00 10.70 7 1476 CA GLN A 184 27.046 82.624 24.601 1.008.62 6 1477 C GLN A 184 26.939 82.844 23.102 1.00 10.69 6 1478 O GLN A184 26.509 81.913 22.388 1.00 10.72 8 1479 CB GLN A 184 25.772 83.07825.330 1.00 12.35 6 1480 CG GLN A 184 25.730 82.584 26.785 1.00 9.80 61481 CD GLN A 184 24.603 83.315 27.538 1.00 12.56 6 1482 OE1 GLN A 18424.739 84.527 27.890 1.00 15.21 8 1483 NE2 GLN A 184 23.536 82.58027.775 1.00 8.78 7 1484 N TRP A 185 27.186 84.018 22.585 1.00 11.90 71485 CA TRP A 185 26.968 84.285 21.148 1.00 9.74 6 1486 C TRP A 18528.252 84.298 20.318 1.00 10.30 6 1487 O TRP A 185 28.093 84.277 19.0651.00 11.67 8 1488 CB TRP A 185 26.201 85.647 20.965 1.00 12.61 6 1489 CGTRP A 185 24.696 85.390 21.039 1.00 10.95 6 1490 CD1 TRP A 185 23.86385.166 19.989 1.00 12.59 6 1491 CD2 TRP A 185 23.898 85.345 22.226 1.0012.07 6 1492 NE1 TRP A 185 22.561 84.887 20.428 1.00 14.15 7 1493 CE2TRP A 185 22.600 85.003 21.805 1.00 13.63 6 1494 CE3 TRP A 185 24.15485.530 23.587 1.00 13.34 6 1495 CZ2 TRP A 185 21.534 84.846 22.703 1.0014.01 6 1496 CZ3 TRP A 185 23.083 85.361 24.494 1.00 14.75 6 1497 CH2TRP A 185 21.812 85.004 24.035 1.00 13.91 6 1498 N LYS A 186 29.41384.254 20.924 1.00 11.31 7 1499 CA LYS A 186 30.655 84.170 20.127 1.0012.29 6 1500 C LYS A 186 31.228 82.764 20.238 1.00 14.72 6 1501 O LYS A186 30.718 81.896 20.981 1.00 12.47 8 1502 CB LYS A 186 31.682 85.22420.582 1.00 11.09 6 1503 CG LYS A 186 31.145 86.646 20.243 1.00 14.74 61504 CD LYS A 186 32.295 87.655 20.601 1.00 14.53 6 1505 CE LYS A 18631.688 89.051 20.286 1.00 20.29 6 1506 NZ LYS A 186 32.744 89.943 19.7261.00 28.67 7 1507 N ASN A 187 32.217 82.446 19.379 1.00 13.16 7 1508 CAASN A 187 32.653 81.074 19.195 1.00 13.22 6 1509 C ASN A 187 33.58780.604 20.314 1.00 15.43 6 1510 O ASN A 187 34.587 81.250 20.646 1.0012.76 8 1511 CB ASN A 187 33.386 80.850 17.862 1.00 12.72 6 1512 CG ASNA 187 32.673 81.537 16.697 1.00 18.84 6 1513 OD1 ASN A 187 31.447 81.45616.631 1.00 15.46 8 1514 ND2 ASN A 187 33.426 82.219 15.839 1.00 16.94 71515 N PHE A 188 33.369 79.356 20.719 1.00 11.91 7 1516 CA PHE A 18834.321 78.658 21.604 1.00 10.93 6 1517 C PHE A 188 35.600 78.457 20.8061.00 13.95 6 1518 O PHE A 188 35.534 78.128 19.632 1.00 13.55 8 1519 CBPHE A 188 33.682 77.259 21.822 1.00 11.05 6 1520 CG PHE A 188 34.17776.552 23.071 1.00 11.08 6 1521 CD1 PHE A 188 35.431 75.953 23.060 1.0014.39 6 1522 CD2 PHE A 188 33.364 76.492 24.194 1.00 14.52 6 1523 CE1PHE A 188 35.865 75.309 24.204 1.00 15.63 6 1524 CE2 PHE A 188 33.82175.818 25.327 1.00 14.28 6 1525 CZ PHE A 188 35.081 75.233 25.350 1.0012.75 6 1526 N THR A 189 36.737 78.710 21.504 1.00 11.89 7 1527 CA THR A189 38.000 78.578 20.769 1.00 11.77 6 1528 C THR A 189 38.851 77.52421.457 1.00 13.65 6 1529 O THR A 189 38.630 77.149 22.589 1.00 14.67 81530 CB THR A 189 38.826 79.904 20.788 1.00 12.56 6 1531 OG1 THR A 18939.066 80.215 22.180 1.00 15.52 8 1532 CG2 THR A 189 38.012 81.04520.136 1.00 13.79 6 1533 N ASP A 190 39.773 76.961 20.639 1.00 11.10 71534 CA ASP A 190 40.736 75.985 21.186 1.00 11.48 6 1535 C ASP A 19042.109 76.575 20.929 1.00 11.63 6 1536 O ASP A 190 42.403 77.103 19.8611.00 13.03 8 1537 CB ASP A 190 40.530 74.703 20.365 1.00 11.07 6 1538 CGASP A 190 41.445 73.591 20.781 1.00 12.55 6 1539 OD1 ASP A 190 42.69173.716 20.943 1.00 14.12 8 1540 OD2 ASP A 190 40.937 72.422 20.956 1.0014.32 8 1541 N PRO A 191 43.013 76.539 21.885 1.00 12.39 7 1542 CA PRO A191 44.344 77.094 21.756 1.00 16.15 6 1543 C PRO A 191 45.205 76.48820.648 1.00 17.03 6 1544 O PRO A 191 46.194 77.139 20.258 1.00 17.33 81545 CB PRO A 191 45.077 76.806 23.067 1.00 15.82 6 1546 CG PRO A 19143.951 76.489 24.024 1.00 19.99 6 1547 CD PRO A 191 42.769 75.960 23.2201.00 15.14 6 1548 N ALA A 192 44.778 75.374 20.102 1.00 12.41 7 1549 CAALA A 192 45.446 74.851 18.871 1.00 16.29 6 1550 C ALA A 192 45.27975.807 17.697 1.00 21.11 6 1551 O ALA A 192 46.014 75.779 16.675 1.0019.85 8 1552 CB ALA A 192 44.978 73.466 18.579 1.00 20.48 6 1553 N GLY A193 44.317 76.695 17.671 1.00 16.93 7 1554 CA GLY A 193 44.199 77.73316.641 1.00 17.03 6 1555 C GLY A 193 42.919 77.582 15.819 1.00 17.85 61556 O GLY A 193 42.991 77.960 14.651 1.00 17.03 8 1557 N PHE A 19441.888 76.955 16.373 1.00 13.47 7 1558 CA PHE A 194 40.612 76.976 15.5671.00 11.84 6 1559 C PHE A 194 39.441 77.265 16.536 1.00 11.03 6 1560 OPHE A 194 39.621 77.423 17.750 1.00 11.69 8 1561 CB PHE A 194 40.41175.629 14.855 1.00 10.98 6 1562 CG PHE A 194 40.568 74.412 15.767 1.0011.46 6 1563 CD1 PHE A 194 39.545 74.063 16.649 1.00 11.56 6 1564 CD2PHE A 194 41.707 73.656 15.747 1.00 15.24 6 1565 CE1 PHE A 194 39.68872.942 17.460 1.00 11.26 6 1566 CE2 PHE A 194 41.871 72.533 16.574 1.0012.49 6 1567 CZ PHE A 194 40.860 72.181 17.450 1.00 12.03 6 1568 N SER A195 38.283 77.497 15.895 1.00 10.73 7 1569 CA SER A 195 37.097 77.78216.704 1.00 11.52 6 1570 C SER A 195 36.081 76.649 16.423 1.00 11.92 61571 O SER A 195 36.284 75.902 15.519 1.00 10.36 8 1572 CB SER A 19536.416 79.059 16.186 1.00 16.30 6 1573 OG SER A 195 37.442 80.119 16.2161.00 22.79 8 1574 N LEU A 196 35.060 76.594 17.262 1.00 12.22 7 1575 CALEU A 196 34.007 75.622 17.060 1.00 12.16 6 1576 C LEU A 196 32.75676.384 16.584 1.00 7.60 6 1577 O LEU A 196 32.364 77.416 17.112 1.0013.16 8 1578 CB LEU A 196 33.660 74.883 18.410 1.00 10.95 6 1579 CG LEUA 196 34.880 74.298 19.107 1.00 10.75 6 1580 CD1 LEU A 196 34.439 73.45420.334 1.00 11.59 6 1581 CD2 LEU A 196 35.719 73.384 18.134 1.00 12.48 61582 N ALA A 197 32.139 75.877 15.481 1.00 9.97 7 1583 CA ALA A 19730.995 76.637 14.905 1.00 10.64 6 1584 C ALA A 197 29.788 76.658 15.8301.00 14.16 6 1585 O ALA A 197 29.362 75.622 16.314 1.00 11.22 8 1586 CBALA A 197 30.629 75.928 13.565 1.00 10.95 6 1587 N ASP A 198 29.42977.869 16.236 1.00 10.28 7 1588 CA ASP A 198 28.459 78.009 17.350 1.0010.50 6 1589 C ASP A 198 27.030 77.880 16.795 1.00 11.99 6 1590 O ASP A198 26.607 78.731 15.993 1.00 13.33 8 1591 CB ASP A 198 28.744 79.43317.900 1.00 12.29 6 1592 CG ASP A 198 28.236 79.529 19.353 1.00 10.72 61593 OD1 ASP A 198 28.683 78.683 20.172 1.00 11.33 8 1594 OD2 ASP A 19827.401 80.452 19.671 1.00 10.45 8 1595 N LEU A 199 26.310 76.847 17.2471.00 10.29 7 1596 CA LEU A 199 24.927 76.690 16.763 1.00 8.80 6 1597 CLEU A 199 24.086 77.821 17.321 1.00 9.88 6 1598 O LEU A 199 24.24678.320 18.449 1.00 11.27 8 1599 CB LEU A 199 24.452 75.296 17.279 1.009.52 6 1600 CG LEU A 199 25.178 74.135 16.526 1.00 10.88 6 1601 CD1 LEUA 199 24.799 72.879 17.321 1.00 12.59 6 1602 CD2 LEU A 199 24.658 74.04515.071 1.00 14.19 6 1603 N SER A 200 23.024 78.144 16.505 1.00 11.57 71604 CA SER A 200 22.055 79.160 16.950 1.00 10.26 6 1605 C SER A 20020.810 78.424 17.499 1.00 11.50 6 1606 O SER A 200 19.994 77.917 16.7411.00 11.79 8 1607 CB SER A 200 21.636 80.012 15.731 1.00 14.77 6 1608 OGSER A 200 20.723 81.011 16.249 1.00 13.69 8 1609 N GLN A 201 20.78678.294 18.837 1.00 10.61 7 1610 CA GLN A 201 19.599 77.668 19.473 1.0011.55 6 1611 C GLN A 201 18.421 78.648 19.371 1.00 11.79 6 1612 O GLN A201 17.305 78.161 19.700 1.00 12.43 8 1613 CB GLN A 201 19.852 77.35920.969 1.00 11.94 6 1614 CG GLN A 201 21.042 76.370 21.151 1.00 10.05 61615 CD GLN A 201 22.393 77.086 21.126 1.00 10.84 6 1616 OE1 GLN A 20122.499 78.298 21.208 1.00 11.60 8 1617 NE2 GLN A 201 23.465 76.23121.079 1.00 9.83 7 1618 N GLU A 202 18.590 79.860 18.862 1.00 10.41 71619 CA GLU A 202 17.434 80.763 18.667 1.00 11.55 6 1620 C GLU A 20216.849 80.531 17.277 1.00 14.51 6 1621 O GLU A 202 15.856 81.166 16.9031.00 16.57 8 1622 CB GLU A 202 17.877 82.226 18.875 1.00 10.69 6 1623 CGGLU A 202 18.522 82.442 20.252 1.00 9.01 6 1624 CD GLU A 202 20.00282.069 20.330 1.00 12.78 6 1625 OE1 GLU A 202 20.680 82.031 19.299 1.0016.62 8 1626 OE2 GLU A 202 20.457 81.782 21.434 1.00 12.31 8 1627 N ASNA 203 17.507 79.704 16.435 1.00 11.04 7 1628 CA ASN A 203 16.939 79.31815.142 1.00 10.64 6 1629 C ASN A 203 16.020 78.098 15.372 1.00 13.48 61630 O ASN A 203 16.441 77.148 16.008 1.00 12.81 8 1631 CB ASN A 20318.105 78.892 14.217 1.00 11.71 6 1632 CG ASN A 203 17.604 78.307 12.9301.00 15.36 6 1633 OD1 ASN A 203 17.271 77.124 12.838 1.00 15.37 8 1634ND2 ASN A 203 17.611 79.108 11.829 1.00 15.33 7 1635 N GLY A 204 14.79778.219 14.831 1.00 13.94 7 1636 CA GLY A 204 13.813 77.115 15.175 1.0014.96 6 1637 C GLY A 204 14.202 75.766 14.593 1.00 12.98 6 1638 O GLY A204 13.891 74.775 15.243 1.00 14.33 8 1639 N THR A 205 14.802 75.70513.401 1.00 11.88 7 1640 CA THR A 205 15.279 74.405 12.894 1.00 12.45 61641 C THR A 205 16.275 73.780 13.856 1.00 11.35 6 1642 O THR A 20516.161 72.621 14.172 1.00 11.84 8 1643 CB THR A 205 15.866 74.603 11.4971.00 14.40 6 1644 OG1 THR A 205 14.760 75.060 10.662 1.00 18.35 8 1645CG2 THR A 205 16.344 73.256 10.930 1.00 16.31 6 1646 N ILE A 206 17.29574.586 14.188 1.00 10.89 7 1647 CA ILE A 206 18.330 73.996 15.081 1.0010.54 6 1648 C ILE A 206 17.736 73.689 16.457 1.00 9.48 6 1649 O ILE A206 18.081 72.638 17.051 1.00 10.61 8 1650 CB ILE A 206 19.481 75.01715.212 1.00 9.16 6 1651 CG1 ILE A 206 20.193 75.155 13.844 1.00 12.29 61652 CG2 ILE A 206 20.550 74.624 16.273 1.00 11.91 6 1653 CD1 ILE A 20620.691 73.847 13.218 1.00 12.69 6 1654 N ALA A 207 16.912 74.562 17.0211.00 10.30 7 1655 CA ALA A 207 16.350 74.185 18.339 1.00 12.45 6 1656 CALA A 207 15.583 72.871 18.311 1.00 12.96 6 1657 O ALA A 207 15.71472.053 19.217 1.00 13.37 8 1658 CB ALA A 207 15.511 75.359 18.883 1.0013.30 6 1659 N GLN A 208 14.749 72.676 17.282 1.00 10.55 7 1660 CA GLN A208 13.968 71.431 17.236 1.00 11.60 6 1661 C GLN A 208 14.842 70.25616.877 1.00 14.22 6 1662 O GLN A 208 14.627 69.200 17.426 1.00 11.79 81663 CB GLN A 208 12.869 71.573 16.136 1.00 13.62 6 1664 CG GLN A 20811.847 70.429 16.197 1.00 14.37 6 1665 CD GLN A 208 11.089 70.392 17.5131.00 15.09 6 1666 OE1 GLN A 208 10.565 71.371 17.957 1.00 14.67 8 1667NE2 GLN A 208 11.168 69.230 18.180 1.00 14.23 7 1668 N TYR A 209 15.87670.454 16.062 1.00 11.41 7 1669 CA TYR A 209 16.807 69.372 15.724 1.0010.71 6 1670 C TYR A 209 17.570 68.930 16.979 1.00 10.31 6 1671 O TYR A209 17.634 67.727 17.231 1.00 11.12 8 1672 CB TYR A 209 17.840 69.98914.743 1.00 11.54 6 1673 CG TYR A 209 19.072 69.148 14.457 1.00 12.56 61674 CD1 TYR A 209 19.031 68.083 13.584 1.00 11.38 6 1675 CD2 TYR A 20920.269 69.485 15.060 1.00 12.87 6 1676 CE1 TYR A 209 20.184 67.34113.286 1.00 16.27 6 1677 CE2 TYR A 209 21.432 68.739 14.794 1.00 13.55 61678 CZ TYR A 209 21.368 67.676 13.915 1.00 13.50 6 1679 OH TYR A 20922.527 66.968 13.654 1.00 14.21 8 1680 N LEU A 210 17.985 69.883 17.8211.00 10.88 7 1681 CA LEU A 210 18.731 69.461 19.027 1.00 10.76 6 1682 CLEU A 210 17.776 68.829 20.049 1.00 11.52 6 1683 O LEU A 210 18.17867.863 20.687 1.00 11.55 8 1684 CB LEU A 210 19.388 70.688 19.713 1.0010.40 6 1685 CG LEU A 210 20.603 71.237 18.893 1.00 10.20 6 1686 CD1 LEUA 210 20.918 72.628 19.480 1.00 12.47 6 1687 CD2 LEU A 210 21.766 70.26018.920 1.00 13.21 6 1688 N THR A 211 16.539 69.327 20.069 1.00 9.66 71689 CA THR A 211 15.520 68.689 20.933 1.00 11.98 6 1690 C THR A 21115.294 67.272 20.496 1.00 11.93 6 1691 O THR A 211 15.311 66.354 21.3351.00 11.42 8 1692 CB THR A 211 14.193 69.502 20.889 1.00 12.29 6 1693OG1 THR A 211 14.488 70.842 21.373 1.00 11.73 8 1694 CG2 THR A 21113.137 68.832 21.808 1.00 10.37 6 1695 N ASP A 212 15.071 67.084 19.1701.00 12.47 7 1696 CA ASP A 212 14.813 65.738 18.671 1.00 10.73 6 1697 CASP A 212 15.998 64.812 18.997 1.00 12.42 6 1698 O ASP A 212 15.74863.598 19.194 1.00 12.22 8 1699 CB ASP A 212 14.605 65.829 17.159 1.0012.33 6 1700 CG ASP A 212 13.253 66.477 16.797 1.00 15.18 6 1701 OD1 ASPA 212 12.379 66.643 17.667 1.00 13.61 8 1702 OD2 ASP A 212 13.100 66.82815.585 1.00 14.64 8 1703 N ALA A 213 17.230 65.326 18.830 1.00 10.02 71704 CA ALA A 213 18.376 64.422 19.084 1.00 10.72 6 1705 C ALA A 21318.422 64.023 20.552 1.00 10.18 6 1706 O ALA A 213 18.819 62.882 20.8611.00 11.96 8 1707 CB ALA A 213 19.679 65.163 18.735 1.00 10.83 6 1708 NALA A 214 18.155 64.970 21.448 1.00 12.55 7 1709 CA ALA A 214 18.18564.599 22.892 1.00 10.81 6 1710 C ALA A 214 17.073 63.631 23.235 1.0011.35 6 1711 O ALA A 214 17.246 62.667 23.953 1.00 12.75 8 1712 CB ALA A214 18.038 65.876 23.757 1.00 10.21 6 1713 N VAL A 215 15.885 63.85422.677 1.00 10.82 7 1714 CA VAL A 215 14.724 62.923 22.875 1.00 11.60 61715 C VAL A 215 15.035 61.577 22.302 1.00 13.68 6 1716 O VAL A 21514.673 60.552 22.903 1.00 15.03 8 1717 CB VAL A 215 13.462 63.523 22.2831.00 14.89 6 1718 CG1 VAL A 215 12.285 62.514 22.234 1.00 16.68 6 1719CG2 VAL A 215 12.982 64.740 23.099 1.00 15.78 6 1720 N GLN A 216 15.75961.496 21.193 1.00 12.25 7 1721 CA GLN A 216 16.153 60.192 20.632 1.0013.52 6 1722 C GLN A 216 17.023 59.404 21.577 1.00 13.62 6 1723 O GLN A216 16.864 58.192 21.706 1.00 12.75 8 1724 CB GLN A 216 16.814 60.38219.232 1.00 12.82 6 1725 CG GLN A 216 17.225 59.032 18.639 1.00 14.36 61726 CD GLN A 216 17.856 59.162 17.261 1.00 18.32 6 1727 OE1 GLN A 21618.762 59.976 16.980 1.00 21.98 8 1728 NE2 GLN A 216 17.392 58.34816.335 1.00 19.07 7 1729 N LEU A 217 17.996 60.043 22.269 1.00 11.16 71730 CA LEU A 217 18.781 59.317 23.261 1.00 11.02 6 1731 C LEU A 21717.885 58.756 24.396 1.00 10.47 6 1732 O LEU A 217 18.106 57.631 24.7541.00 13.19 8 1733 CB LEU A 217 19.847 60.252 23.876 1.00 12.00 6 1734 CGLEU A 217 20.974 60.577 22.859 1.00 10.07 6 1735 CD1 LEU A 217 21.77061.789 23.418 1.00 10.56 6 1736 CD2 LEU A 217 21.953 59.383 22.787 1.0012.18 6 1737 N VAL A 218 16.940 59.584 24.844 1.00 10.50 7 1738 CA VAL A218 16.027 59.030 25.884 1.00 14.12 6 1739 C VAL A 218 15.114 57.91825.304 1.00 12.90 6 1740 O VAL A 218 14.914 56.898 25.978 1.00 14.29 81741 CB VAL A 218 15.121 60.168 26.376 1.00 11.91 6 1742 CG1 VAL A 21814.131 59.671 27.428 1.00 14.89 6 1743 CG2 VAL A 218 16.045 61.16927.107 1.00 14.59 6 1744 N ALA A 219 14.717 57.992 24.051 1.00 14.93 71745 CA ALA A 219 13.868 56.915 23.478 1.00 14.21 6 1746 C ALA A 21914.647 55.619 23.377 1.00 16.64 6 1747 O ALA A 219 14.072 54.517 23.4011.00 14.94 8 1748 CB ALA A 219 13.379 57.270 22.059 1.00 15.54 6 1749 NHIS A 220 15.959 55.702 23.258 1.00 12.54 7 1750 CA HIS A 220 16.85354.570 23.215 1.00 14.41 6 1751 C HIS A 220 17.305 54.124 24.611 1.0012.25 6 1752 O HIS A 220 18.194 53.243 24.711 1.00 13.99 8 1753 CB HIS A220 18.055 54.802 22.293 1.00 11.69 6 1754 CG HIS A 220 17.630 54.76020.840 1.00 14.69 6 1755 ND1 HIS A 220 17.984 53.694 20.064 1.00 14.71 71756 CD2 HIS A 220 16.928 55.624 20.077 1.00 16.42 6 1757 CE1 HIS A 22017.518 53.916 18.823 1.00 16.42 6 1758 NE2 HIS A 220 16.855 55.07718.794 1.00 17.85 7 1759 N GLY A 221 16.735 54.666 25.655 1.00 11.47 71760 CA GLY A 221 16.964 54.129 26.999 1.00 11.21 6 1761 C GLY A 22117.655 55.060 27.965 1.00 13.22 6 1762 O GLY A 221 17.875 54.635 29.0951.00 13.24 8 1763 N ALA A 222 18.297 56.111 27.426 1.00 12.29 7 1764 CAALA A 222 19.139 56.912 28.356 1.00 14.03 6 1765 C ALA A 222 18.32557.381 29.553 1.00 13.32 6 1766 O ALA A 222 17.138 57.794 29.459 1.0010.61 8 1767 CB ALA A 222 19.700 58.136 27.618 1.00 12.95 6 1768 N ASP A223 19.009 57.376 30.709 1.00 11.67 7 1769 CA ASP A 223 18.391 57.76831.951 1.00 10.83 6 1770 C ASP A 223 18.621 59.249 32.306 1.00 12.58 61771 O ASP A 223 18.116 59.667 33.356 1.00 11.47 8 1772 CB ASP A 22318.997 56.964 33.123 1.00 9.67 6 1773 CG ASP A 223 18.744 55.469 32.9251.00 12.72 6 1774 OD1 ASP A 223 17.554 55.095 33.224 1.00 15.35 8 1775OD2 ASP A 223 19.610 54.686 32.482 1.00 10.77 8 1776 N GLY A 224 19.18659.972 31.348 1.00 11.00 7 1777 CA GLY A 224 19.393 61.413 31.651 1.0011.62 6 1778 C GLY A 224 20.641 61.861 30.809 1.00 9.62 6 1779 O GLY A224 21.069 61.107 29.928 1.00 9.69 8 1780 N LEU A 225 20.869 63.12330.983 1.00 10.32 7 1781 CA LEU A 225 21.962 63.749 30.177 1.00 9.63 61782 C LEU A 225 22.828 64.566 31.128 1.00 10.99 6 1783 O LEU A 22522.356 65.110 32.097 1.00 10.86 8 1784 CB LEU A 225 21.389 64.780 29.1721.00 9.89 6 1785 CG LEU A 225 20.424 64.212 28.122 1.00 10.00 6 1786 CD1LEU A 225 19.806 65.361 27.279 1.00 12.69 6 1787 CD2 LEU A 225 21.00363.092 27.243 1.00 13.97 6 1788 N ARG A 226 24.135 64.671 30.790 1.0010.52 7 1789 CA ARG A 226 24.993 65.777 31.295 1.00 9.01 6 1790 C ARG A226 25.093 66.744 30.110 1.00 10.97 6 1791 O ARG A 226 25.628 66.34829.083 1.00 10.94 8 1792 CB ARG A 226 26.337 65.159 31.691 1.00 9.10 61793 CG ARG A 226 27.381 66.213 32.158 1.00 8.52 6 1794 CD ARG A 22628.248 66.648 30.956 1.00 9.82 6 1795 NE ARG A 226 29.438 67.400 31.4251.00 9.22 7 1796 CZ ARG A 226 30.251 68.074 30.592 1.00 9.27 6 1797 NH1ARG A 226 29.978 68.191 29.289 1.00 9.46 7 1798 NH2 ARG A 226 31.31168.687 31.114 1.00 10.94 7 1799 N ILE A 227 24.590 67.940 30.262 1.0010.46 7 1800 CA ILE A 227 24.553 68.901 29.124 1.00 7.87 6 1801 C ILE A227 25.807 69.751 29.238 1.00 8.86 6 1802 O ILE A 227 26.042 70.45030.199 1.00 11.29 8 1803 CB ILE A 227 23.295 69.783 29.269 1.00 9.62 61804 CG1 ILE A 227 22.096 68.814 29.378 1.00 10.28 6 1805 CG2 ILE A 22723.196 70.601 27.964 1.00 11.21 6 1806 CD1 ILE A 227 20.743 69.54729.412 1.00 15.31 6 1807 N ASP A 228 26.544 69.672 28.125 1.00 9.30 71808 CA ASP A 228 27.846 70.399 28.079 1.00 9.30 6 1809 C ASP A 22827.672 71.915 27.904 1.00 9.50 6 1810 O ASP A 228 26.757 72.338 27.1891.00 9.88 8 1811 CB ASP A 228 28.521 69.865 26.769 1.00 9.23 6 1812 CGASP A 228 29.904 70.442 26.587 1.00 10.24 6 1813 OD1 ASP A 228 30.72570.228 27.505 1.00 10.28 8 1814 OD2 ASP A 228 30.208 71.128 25.574 1.009.89 8 1815 N ALA A 229 28.575 72.633 28.582 1.00 8.93 7 1816 CA ALA A229 28.745 74.068 28.257 1.00 9.72 6 1817 C ALA A 229 27.455 74.86828.324 1.00 10.58 6 1818 O ALA A 229 27.123 75.695 27.464 1.00 10.73 81819 CB ALA A 229 29.355 74.180 26.841 1.00 9.90 6 1820 N VAL A 23026.729 74.708 29.487 1.00 9.05 7 1821 CA VAL A 230 25.421 75.392 29.5481.00 9.09 6 1822 C VAL A 230 25.547 76.905 29.753 1.00 10.83 6 1823 OVAL A 230 24.587 77.636 29.573 1.00 12.48 8 1824 CB VAL A 230 24.46974.836 30.634 1.00 10.80 6 1825 CG1 VAL A 230 24.119 73.389 30.262 1.009.84 6 1826 CG2 VAL A 230 25.084 74.934 32.047 1.00 11.19 6 1827 N LYS A231 26.753 77.312 30.189 1.00 9.10 7 1828 CA LYS A 231 26.988 78.76330.234 1.00 7.91 6 1829 C LYS A 231 27.304 79.391 28.883 1.00 11.01 61830 O LYS A 231 27.398 80.604 28.809 1.00 13.02 8 1831 CB LYS A 23128.173 79.043 31.209 1.00 10.48 6 1832 CG LYS A 231 29.567 78.801 30.6021.00 10.63 6 1833 CD LYS A 231 30.599 78.817 31.758 1.00 13.70 6 1834 CELYS A 231 30.937 80.205 32.236 1.00 13.75 6 1835 NZ LYS A 231 32.21580.157 33.104 1.00 11.49 7 1836 N HIS A 232 27.364 78.589 27.814 1.009.37 7 1837 CA HIS A 232 27.744 79.081 26.480 1.00 12.72 6 1838 C HIS A232 26.576 79.044 25.537 1.00 12.48 6 1839 O HIS A 232 26.698 79.50524.388 1.00 9.62 8 1840 CB HIS A 232 28.849 78.129 25.915 1.00 9.94 61841 CG HIS A 232 30.145 78.345 26.709 1.00 9.35 6 1842 ND1 HIS A 23230.780 79.598 26.674 1.00 11.03 7 1843 CD2 HIS A 232 30.803 77.53027.554 1.00 11.85 6 1844 CE1 HIS A 232 31.838 79.483 27.513 1.00 12.22 61845 NE2 HIS A 232 31.882 78.243 28.049 1.00 11.68 7 1846 N PHE A 23325.342 78.757 25.941 1.00 9.67 7 1847 CA PHE A 233 24.165 78.957 25.0621.00 10.57 6 1848 C PHE A 233 23.015 79.437 25.991 1.00 9.21 6 1849 OPHE A 233 23.073 79.254 27.225 1.00 11.50 8 1850 CB PHE A 233 23.79277.705 24.296 1.00 9.50 6 1851 CG PHE A 233 23.382 76.523 25.145 1.0010.66 6 1852 CD1 PHE A 233 24.335 75.588 25.559 1.00 12.13 6 1853 CD2PHE A 233 22.023 76.331 25.466 1.00 11.40 6 1854 CE1 PHE A 233 23.98274.503 26.347 1.00 12.18 6 1855 CE2 PHE A 233 21.642 75.219 26.237 1.0010.50 6 1856 CZ PHE A 233 22.629 74.340 26.657 1.00 11.82 6 1857 N ASN A234 22.051 80.148 25.349 1.00 12.13 7 1858 CA ASN A 234 21.093 80.79926.253 1.00 8.31 6 1859 C ASN A 234 20.367 79.859 27.214 1.00 9.45 61860 O ASN A 234 20.112 78.722 26.829 1.00 9.94 8 1861 CB ASN A 23420.132 81.662 25.369 1.00 10.71 6 1862 CG ASN A 234 18.981 80.871 24.7401.00 12.93 6 1863 OD1 ASN A 234 18.070 80.516 25.519 1.00 12.50 8 1864ND2 ASN A 234 18.975 80.590 23.448 1.00 10.79 7 1865 N SER A 235 20.02380.451 28.374 1.00 10.78 7 1866 CA SER A 235 19.401 79.586 29.396 1.008.67 6 1867 C SER A 235 17.906 79.375 29.177 1.00 11.06 6 1868 O SER A235 17.399 78.402 29.759 1.00 11.56 8 1869 CB ASER A 235 19.594 80.19630.792 0.60 11.41 6 1870 OG ASER A 235 20.974 80.269 31.098 0.60 10.81 81869 CB BSER A 235 19.679 80.067 30.817 0.40 10.03 6 1870 OG BSER A 23519.311 81.423 30.914 0.40 7.85 8 1871 N GLY A 236 17.301 80.140 28.3121.00 10.81 7 1872 CA GLY A 236 15.906 79.857 27.882 1.00 11.83 6 1873 CGLY A 236 15.821 78.448 27.289 1.00 12.34 6 1874 O GLY A 236 14.94277.638 27.552 1.00 11.07 8 1875 N PHE A 237 16.742 78.158 26.370 1.0010.75 7 1876 CA PHE A 237 16.793 76.864 25.702 1.00 9.60 6 1877 C PHE A237 17.034 75.738 26.715 1.00 10.90 6 1878 O PHE A 237 16.476 74.64126.526 1.00 10.74 8 1879 CB PHE A 237 17.714 76.891 24.467 1.00 12.14 61880 CG PHE A 237 17.642 75.595 23.691 1.00 12.02 6 1881 CD1 PHE A 23716.442 75.242 23.048 1.00 12.55 6 1882 CD2 PHE A 237 18.751 74.74023.659 1.00 11.64 6 1883 CE1 PHE A 237 16.367 74.046 22.358 1.00 12.60 61884 CE2 PHE A 237 18.634 73.533 22.952 1.00 11.39 6 1885 CZ PHE A 23717.468 73.200 22.301 1.00 13.43 6 1886 N SER A 238 17.965 75.939 27.6581.00 10.56 7 1887 CA SER A 238 18.119 74.844 28.637 1.00 11.43 6 1888 CSER A 238 16.762 74.489 29.289 1.00 10.24 6 1889 O SER A 238 16.41673.312 29.442 1.00 10.58 8 1890 CB SER A 238 19.069 75.303 29.776 1.0011.86 6 1891 OG SER A 238 20.432 75.070 29.404 1.00 12.16 8 1892 N LYS A239 16.053 75.523 29.757 1.00 10.06 7 1893 CA LYS A 239 14.749 75.26230.433 1.00 10.43 6 1894 C LYS A 239 13.712 74.684 29.505 1.00 10.95 61895 O LYS A 239 13.006 73.718 29.879 1.00 11.91 8 1896 CB LYS A 23914.259 76.598 31.123 1.00 8.56 6 1897 CG LYS A 239 12.889 76.329 31.8611.00 12.08 6 1898 CD LYS A 239 12.577 77.644 32.648 1.00 11.14 6 1899 CELYS A 239 11.131 77.442 33.240 1.00 11.14 6 1900 NZ LYS A 239 10.79778.668 34.098 1.00 10.40 7 1901 N SER A 240 13.600 75.153 28.279 1.009.61 7 1902 CA SER A 240 12.611 74.583 27.330 1.00 9.08 6 1903 C SER A240 13.006 73.207 26.957 1.00 10.90 6 1904 O SER A 240 12.160 72.32026.790 1.00 10.77 8 1905 CB SER A 240 12.560 75.572 26.136 1.00 11.38 61906 OG SER A 240 11.488 75.039 25.266 1.00 12.68 8 1907 N LEU A 24114.300 72.896 26.747 1.00 10.43 7 1908 CA LEU A 241 14.726 71.560 26.3891.00 10.29 6 1909 C LEU A 241 14.420 70.599 27.539 1.00 11.73 6 1910 OLEU A 241 13.924 69.507 27.303 1.00 11.15 8 1911 CB LEU A 241 16.25571.582 26.077 1.00 10.07 6 1912 CG LEU A 241 16.816 70.170 25.829 1.0012.71 6 1913 CD1 LEU A 241 16.205 69.502 24.577 1.00 13.39 6 1914 CD2LEU A 241 18.333 70.350 25.611 1.00 12.90 6 1915 N ALA A 242 14.71071.055 28.778 1.00 11.25 7 1916 CA ALA A 242 14.427 70.181 29.912 1.0010.06 6 1917 C ALA A 242 12.923 69.852 29.969 1.00 10.68 6 1918 O ALA A242 12.565 68.703 30.215 1.00 10.97 8 1919 CB ALA A 242 14.910 70.88931.196 1.00 10.49 6 1920 N ASP A 243 12.062 70.870 29.712 1.00 10.40 71921 CA ASP A 243 10.609 70.595 29.694 1.00 11.54 6 1922 C ASP A 24310.365 69.448 28.700 1.00 12.78 6 1923 O ASP A 243 9.636 68.474 29.0061.00 12.31 8 1924 CB ASP A 243 9.930 71.904 29.186 1.00 11.95 6 1925 CGASP A 243 8.507 71.717 28.674 1.00 13.21 6 1926 OD1 ASP A 243 7.66871.113 29.422 1.00 12.98 8 1927 OD2 ASP A 243 8.223 72.178 27.546 1.0012.92 8 1928 N LYS A 244 10.825 69.536 27.451 1.00 10.42 7 1929 CA LYS A244 10.523 68.449 26.484 1.00 10.94 6 1930 C LYS A 244 10.997 67.09726.998 1.00 13.31 6 1931 O LYS A 244 10.349 66.061 26.763 1.00 12.24 81932 CB LYS A 244 11.232 68.728 25.122 1.00 11.69 6 1933 CG LYS A 24410.924 70.142 24.580 1.00 14.16 6 1934 CD LYS A 244 9.398 70.400 24.4831.00 13.14 6 1935 CE LYS A 244 9.129 71.869 24.133 1.00 13.82 6 1936 NZLYS A 244 9.582 72.780 25.269 1.00 12.11 7 1937 N LEU A 245 12.21367.068 27.593 1.00 11.20 7 1938 CA LEU A 245 12.730 65.762 28.039 1.0011.98 6 1939 C LEU A 245 11.936 65.200 29.205 1.00 12.96 6 1940 O LEU A245 11.665 63.996 29.219 1.00 12.16 8 1941 CB LEU A 245 14.221 65.96128.461 1.00 10.88 6 1942 CG LEU A 245 15.091 66.282 27.206 1.00 15.60 61943 CD1 LEU A 245 16.493 66.701 27.692 1.00 14.87 6 1944 CD2 LEU A 24515.227 65.052 26.282 1.00 19.24 6 1945 N TYR A 246 11.480 66.037 30.1361.00 11.31 7 1946 CA TYR A 246 10.676 65.529 31.258 1.00 11.13 6 1947 CTYR A 246 9.294 65.090 30.770 1.00 11.59 6 1948 O TYR A 246 8.674 64.30631.500 1.00 13.03 8 1949 CB TYR A 246 10.582 66.586 32.359 1.00 12.53 61950 CG TYR A 246 11.928 66.907 32.995 1.00 9.85 6 1951 CD1 TYR A 24612.882 65.941 33.210 1.00 11.79 6 1952 CD2 TYR A 246 12.163 68.22833.408 1.00 10.52 6 1953 CE1 TYR A 246 14.103 66.245 33.830 1.00 11.71 61954 CE2 TYR A 246 13.379 68.569 34.021 1.00 10.59 6 1955 CZ TYR A 24614.319 67.562 34.208 1.00 11.60 6 1956 OH TYR A 246 15.536 67.856 34.8161.00 11.49 8 1957 N GLN A 247 8.769 65.623 29.672 1.00 12.54 7 1958 CAGLN A 247 7.501 65.088 29.112 1.00 13.07 6 1959 C GLN A 247 7.677 63.69028.587 1.00 13.75 6 1960 O GLN A 247 6.712 62.875 28.651 1.00 16.16 81961 CB GLN A 247 7.016 66.001 27.940 1.00 12.33 6 1962 CG GLN A 2476.530 67.357 28.518 1.00 13.62 6 1963 CD GLN A 247 6.016 68.220 27.3971.00 16.89 6 1964 OE1 GLN A 247 5.355 67.699 26.462 1.00 18.89 8 1965NE2 GLN A 247 6.372 69.518 27.387 1.00 14.76 7 1966 N LYS A 248 8.88163.349 28.162 1.00 14.17 7 1967 CA LYS A 248 9.163 61.979 27.702 1.0015.18 6 1968 C LYS A 248 9.328 61.000 28.836 1.00 15.52 6 1969 O LYS A248 8.839 59.868 28.746 1.00 16.45 8 1970 CB ALYS A 248 10.397 61.99426.793 0.50 13.40 6 1971 CG ALYS A 248 10.116 62.793 25.528 0.50 14.14 61972 CD ALYS A 248 8.958 62.165 24.749 0.50 17.69 6 1973 CE ALYS A 2488.449 63.068 23.657 0.50 18.41 6 1974 NZ ALYS A 248 7.682 62.378 22.5770.50 25.68 7 1970 CB BLYS A 248 10.414 62.030 26.816 0.50 17.60 6 1971CG BLYS A 248 10.840 60.676 26.292 0.50 22.20 6 1972 CD BLYS A 24811.561 60.755 24.977 0.50 29.85 6 1973 CE BLYS A 248 11.495 59.49724.150 0.50 18.09 6 1974 NZ BLYS A 248 10.779 58.367 24.885 0.50 21.86 71975 N LYS A 249 10.131 61.400 29.830 1.00 12.97 7 1976 CA LYS A 24910.424 60.442 30.917 1.00 14.04 6 1977 C LYS A 249 10.983 61.213 32.0841.00 11.94 6 1978 O LYS A 249 11.520 62.316 31.876 1.00 13.26 8 1979 CBLYS A 249 11.514 59.423 30.462 1.00 15.09 6 1980 CG LYS A 249 11.67458.358 31.542 1.00 15.17 6 1981 CD LYS A 249 12.552 57.175 31.147 1.0023.08 6 1982 CE LYS A 249 12.451 56.111 32.249 1.00 27.89 6 1983 NZ LYSA 249 13.149 54.836 31.875 1.00 36.10 7 1984 N ASP A 250 10.870 60.67833.288 1.00 11.41 7 1985 CA ASP A 250 11.406 61.336 34.494 1.00 12.04 61986 C ASP A 250 12.918 61.011 34.626 1.00 11.51 6 1987 O ASP A 25013.348 60.354 35.546 1.00 13.89 8 1988 CB ASP A 250 10.638 60.891 35.7281.00 11.54 6 1989 CG ASP A 250 10.618 59.405 36.030 1.00 15.08 6 1990OD1 ASP A 250 10.695 58.618 35.085 1.00 15.58 8 1991 OD2 ASP A 25010.448 59.027 37.224 1.00 15.73 8 1992 N ILE A 251 13.644 61.541 33.6071.00 11.19 7 1993 CA ILE A 251 15.093 61.346 33.593 1.00 12.04 6 1994 CILE A 251 15.777 62.413 34.467 1.00 12.14 6 1995 O ILE A 251 15.14863.303 34.990 1.00 13.37 8 1996 CB ILE A 251 15.610 61.331 32.164 1.0015.29 6 1997 CG1 ILE A 251 14.988 62.477 31.361 1.00 23.77 6 1998 CG2ILE A 251 15.204 60.064 31.402 1.00 16.73 6 1999 CD1 ILE A 251 15.64563.784 31.503 1.00 25.03 6 2000 N PHE A 252 17.122 62.248 34.639 1.009.99 7 2001 CA PHE A 252 17.885 63.182 35.420 1.00 9.59 6 2002 C PHE A252 18.690 64.105 34.501 1.00 11.26 6 2003 O PHE A 252 19.347 63.58733.596 1.00 12.38 8 2004 CB PHE A 252 18.916 62.372 36.275 1.00 13.00 62005 CG PHE A 252 19.748 63.290 37.145 1.00 11.27 6 2006 CD1 PHE A 25219.182 63.951 38.241 1.00 12.24 6 2007 CD2 PHE A 252 21.094 63.49436.838 1.00 12.52 6 2008 CE1 PHE A 252 19.907 64.802 39.029 1.00 11.05 62009 CE2 PHE A 252 21.843 64.327 37.664 1.00 11.26 6 2010 CZ PHE A 25221.263 65.031 38.750 1.00 10.84 6 2011 N LEU A 253 18.740 65.389 34.7721.00 12.09 7 2012 CA LEU A 253 19.592 66.278 33.936 1.00 9.30 6 2013 CLEU A 253 20.498 67.083 34.913 1.00 9.94 6 2014 O LEU A 253 20.09467.647 35.914 1.00 11.26 8 2015 CB LEU A 253 18.694 67.378 33.282 1.008.72 6 2016 CG LEU A 253 17.749 66.766 32.216 1.00 10.91 6 2017 CD1 LEUA 253 16.881 67.891 31.562 1.00 10.35 6 2018 CD2 LEU A 253 18.508 66.05131.089 1.00 12.13 6 2019 N VAL A 254 21.761 67.179 34.422 1.00 11.23 72020 CA VAL A 254 22.750 68.015 35.077 1.00 11.09 6 2021 C VAL A 25423.423 68.807 33.921 1.00 10.26 6 2022 O VAL A 254 23.707 68.196 32.8921.00 10.32 8 2023 CB VAL A 254 23.722 67.184 35.947 1.00 9.61 6 2024 CG1VAL A 254 24.552 66.161 35.161 1.00 10.99 6 2025 CG2 VAL A 254 24.68868.131 36.685 1.00 11.22 6 2026 N GLY A 255 23.762 70.047 34.194 1.0010.96 7 2027 CA GLY A 255 24.492 70.879 33.243 1.00 11.43 6 2028 C GLY A255 25.877 71.193 33.731 1.00 11.23 6 2029 O GLY A 255 26.095 71.40434.967 1.00 10.31 8 2030 N GLU A 256 26.828 71.308 32.765 1.00 10.72 72031 CA GLU A 256 28.159 71.786 33.187 1.00 10.84 6 2032 C GLU A 25628.236 73.315 33.013 1.00 11.33 6 2033 O GLU A 256 28.295 73.820 31.8711.00 10.36 8 2034 CB GLU A 256 29.172 71.178 32.167 1.00 10.52 6 2035 CGGLU A 256 30.603 71.617 32.605 1.00 10.70 6 2036 CD GLU A 256 31.44272.059 31.414 1.00 11.32 6 2037 OE1 GLU A 256 30.925 72.467 30.347 1.0010.78 8 2038 OE2 GLU A 256 32.696 71.998 31.517 1.00 11.88 8 2039 N TRPA 257 28.173 74.038 34.120 1.00 9.79 7 2040 CA TRP A 257 28.409 75.48034.158 1.00 9.57 6 2041 C TRP A 257 29.798 75.608 34.799 1.00 10.84 62042 O TRP A 257 29.908 75.560 36.037 1.00 10.82 8 2043 CB TRP A 25727.301 76.175 34.997 1.00 9.83 6 2044 CG TRP A 257 27.449 77.700 34.8541.00 8.59 6 2045 CD1 TRP A 257 28.566 78.442 35.196 1.00 12.90 6 2046CD2 TRP A 257 26.431 78.592 34.412 1.00 10.35 6 2047 NE1 TRP A 25728.295 79.753 34.937 1.00 12.55 7 2048 CE2 TRP A 257 27.020 79.89134.459 1.00 12.29 6 2049 CE3 TRP A 257 25.124 78.425 33.946 1.00 13.94 62050 CZ2 TRP A 257 26.317 81.041 34.055 1.00 10.73 6 2051 CZ3 TRP A 25724.385 79.544 33.527 1.00 13.32 6 2052 CH2 TRP A 257 25.026 80.79333.599 1.00 11.64 6 2053 N TYR A 258 30.831 75.725 33.986 1.00 11.79 72054 CA TYR A 258 32.211 75.619 34.524 1.00 11.80 6 2055 C TYR A 25832.527 76.859 35.355 1.00 12.06 6 2056 O TYR A 258 32.370 77.988 34.8691.00 13.57 8 2057 CB TYR A 258 33.189 75.508 33.335 1.00 11.31 6 2058 CGTYR A 258 34.562 74.978 33.723 1.00 11.97 6 2059 CD1 TYR A 258 35.45275.687 34.524 1.00 13.71 6 2060 CD2 TYR A 258 34.932 73.734 33.234 1.0011.78 6 2061 CE1 TYR A 258 36.707 75.160 34.859 1.00 15.77 6 2062 CE2TYR A 258 36.179 73.226 33.564 1.00 13.38 6 2063 CZ TYR A 258 37.03773.908 34.376 1.00 16.44 6 2064 OH TYR A 258 38.277 73.304 34.631 1.0020.59 8 2065 N GLY A 259 33.030 76.605 36.550 1.00 9.86 7 2066 CA GLY A259 33.584 77.705 37.361 1.00 12.24 6 2067 C GLY A 259 32.510 78.69037.891 1.00 11.55 6 2068 O GLY A 259 31.417 78.276 38.227 1.00 12.61 82069 N ASP A 260 32.921 79.963 37.891 1.00 11.45 7 2070 CA ASP A 26032.064 81.004 38.486 1.00 10.59 6 2071 C ASP A 260 31.718 80.614 39.9471.00 12.08 6 2072 O ASP A 260 30.554 80.528 40.317 1.00 11.34 8 2073 CBASP A 260 30.792 81.286 37.665 1.00 13.01 6 2074 CG ASP A 260 31.16081.807 36.269 1.00 16.43 6 2075 OD1 ASP A 260 32.136 82.593 36.148 1.0013.58 8 2076 OD2 ASP A 260 30.486 81.502 35.274 1.00 14.47 8 2077 N ASPA 261 32.812 80.528 40.708 1.00 10.89 7 2078 CA ASP A 261 32.709 80.23942.158 1.00 13.96 6 2079 C ASP A 261 32.059 81.369 42.936 1.00 12.00 62080 O ASP A 261 31.920 82.528 42.502 1.00 13.08 8 2081 CB ASP A 26134.125 79.875 42.610 1.00 17.34 6 2082 CG ASP A 261 34.615 78.518 42.0741.00 18.47 6 2083 OD1 ASP A 261 33.990 77.881 41.181 1.00 22.23 8 2084OD2 ASP A 261 35.642 78.035 42.569 1.00 20.46 8 2085 N PRO A 262 31.75181.124 44.230 1.00 11.36 7 2086 CA PRO A 262 31.155 82.197 45.033 1.0013.50 6 2087 C PRO A 262 32.085 83.428 45.042 1.00 15.27 6 2088 O PRO A262 33.325 83.254 45.078 1.00 17.80 8 2089 CB PRO A 262 30.973 81.58346.445 1.00 14.74 6 2090 CG PRO A 262 30.818 80.086 46.071 1.00 13.76 62091 CD PRO A 262 31.873 79.856 44.938 1.00 11.66 6 2092 N GLY A 26331.385 84.560 45.069 1.00 20.11 7 2093 CA GLY A 263 32.178 85.810 45.0911.00 20.82 6 2094 C GLY A 263 32.444 86.343 43.693 1.00 22.93 6 2095 OGLY A 263 33.030 87.433 43.565 1.00 26.12 8 2096 N THR A 264 32.20485.581 42.640 1.00 16.30 7 2097 CA THR A 264 32.579 85.990 41.270 1.0015.29 6 2098 C THR A 264 31.378 86.647 40.599 1.00 14.14 6 2099 O THR A264 30.225 86.490 41.019 1.00 15.14 8 2100 CB THR A 264 33.154 84.89040.377 1.00 17.00 6 2101 OG1 THR A 264 32.185 83.864 40.214 1.00 17.20 82102 CG2 THR A 264 34.455 84.302 40.998 1.00 18.53 6 2103 N ALA A 26531.684 87.407 39.536 1.00 14.47 7 2104 CA ALA A 265 30.579 88.206 38.9571.00 16.68 6 2105 C ALA A 265 29.455 87.387 38.348 1.00 14.50 6 2106 OALA A 265 28.315 87.921 38.316 1.00 15.71 8 2107 CB ALA A 265 31.15389.034 37.793 1.00 18.93 6 2108 N ASN A 266 29.808 86.186 37.837 1.0011.26 7 2109 CA ASN A 266 28.739 85.402 37.199 1.00 12.93 6 2110 C ASN A266 28.140 84.338 38.110 1.00 13.52 6 2111 O ASN A 266 27.364 83.48437.632 1.00 11.82 8 2112 CB ASN A 266 29.289 84.792 35.855 1.00 15.03 62113 CG ASN A 266 29.632 85.944 34.889 1.00 15.26 6 2114 OD1 ASN A 26628.938 86.955 34.822 1.00 13.24 8 2115 ND2 ASN A 266 30.698 85.79734.146 1.00 14.64 7 2116 N HIS A 267 28.621 84.306 39.353 1.00 12.23 72117 CA HIS A 267 28.106 83.276 40.271 1.00 13.10 6 2118 C HIS A 26726.596 83.276 40.469 1.00 13.44 6 2119 O HIS A 267 25.999 82.182 40.3991.00 12.11 8 2120 CB HIS A 267 28.852 83.439 41.616 1.00 10.82 6 2121 CGHIS A 267 28.469 82.306 42.563 1.00 12.37 6 2122 ND1 HIS A 267 28.87781.020 42.410 1.00 11.65 7 2123 CD2 HIS A 267 27.637 82.360 43.640 1.0015.29 6 2124 CE1 HIS A 267 28.355 80.278 43.375 1.00 12.97 6 2125 NE2HIS A 267 27.608 81.080 44.153 1.00 11.63 7 2126 N LEU A 268 26.00184.430 40.726 1.00 10.81 7 2127 CA LEU A 268 24.548 84.455 40.988 1.0013.40 6 2128 C LEU A 268 23.766 83.997 39.768 1.00 11.02 6 2129 O LEU A268 22.745 83.268 39.957 1.00 12.74 8 2130 CB LEU A 268 24.169 85.88941.374 1.00 14.95 6 2131 CG LEU A 268 22.599 86.052 41.471 1.00 19.99 62132 CD1 LEU A 268 22.040 85.151 42.563 1.00 24.25 6 2133 CD2 LEU A 26822.298 87.536 41.677 1.00 25.18 6 2134 N GLU A 269 24.210 84.274 38.5491.00 11.51 7 2135 CA GLU A 269 23.495 83.760 37.381 1.00 11.81 6 2136 CGLU A 269 23.525 82.221 37.386 1.00 10.11 6 2137 O GLU A 269 22.51281.596 37.067 1.00 11.07 8 2138 CB GLU A 269 24.190 84.360 36.122 1.0013.26 6 2139 CG GLU A 269 23.490 83.803 34.867 1.00 11.45 6 2140 CD GLUA 269 24.122 84.417 33.582 1.00 13.11 6 2141 OE1 GLU A 269 24.906 85.36933.643 1.00 12.92 8 2142 OE2 GLU A 269 23.720 83.906 32.525 1.00 12.17 82143 N LYS A 270 24.678 81.608 37.720 1.00 9.00 7 2144 CA LYS A 27024.754 80.156 37.787 1.00 9.72 6 2145 C LYS A 270 23.806 79.578 38.8621.00 10.98 6 2146 O LYS A 270 23.079 78.613 38.609 1.00 10.64 8 2147 CBLYS A 270 26.221 79.709 38.063 1.00 10.49 6 2148 CG LYS A 270 26.25978.174 38.299 1.00 10.05 6 2149 CD LYS A 270 27.725 77.682 38.502 1.008.77 6 2150 CE LYS A 270 28.236 78.181 39.869 1.00 9.57 6 2151 NZ LYS A270 29.600 77.515 40.161 1.00 11.56 7 2152 N VAL A 271 23.765 80.21840.038 1.00 11.90 7 2153 CA VAL A 271 22.847 79.712 41.105 1.00 10.97 62154 C VAL A 271 21.392 79.835 40.608 1.00 10.81 6 2155 O VAL A 27120.583 78.951 40.827 1.00 11.67 8 2156 CB VAL A 271 23.044 80.608 42.3461.00 13.53 6 2157 CG1 VAL A 271 22.016 80.248 43.435 1.00 12.11 6 2158CG2 VAL A 271 24.455 80.307 42.888 1.00 12.46 6 2159 N ARG A 272 21.06480.978 39.983 1.00 11.20 7 2160 CA ARG A 272 19.668 81.127 39.458 1.0011.53 6 2161 C ARG A 272 19.328 80.041 38.439 1.00 10.29 6 2162 O ARG A272 18.208 79.506 38.389 1.00 11.34 8 2163 CB ARG A 272 19.462 82.54038.859 1.00 9.74 6 2164 CG ARG A 272 19.220 83.552 40.027 1.00 11.97 62165 CD ARG A 272 19.405 85.000 39.483 1.00 10.96 6 2166 NE ARG A 27218.600 85.394 38.306 1.00 12.10 7 2167 CZ ARG A 272 17.297 85.759 38.3771.00 14.61 6 2168 NH1 ARG A 272 16.541 85.765 39.493 1.00 12.14 7 2169NH2 ARG A 272 16.734 86.132 37.232 1.00 12.07 7 2170 N TYR A 273 20.32979.790 37.553 1.00 10.33 7 2171 CA TYR A 273 20.116 78.669 36.589 1.0011.57 6 2172 C TYR A 273 19.882 77.355 37.328 1.00 9.14 6 2173 O TYR A273 18.931 76.590 36.993 1.00 12.29 8 2174 CB TYR A 273 21.415 78.56935.742 1.00 9.07 6 2175 CG TYR A 273 21.388 77.445 34.693 1.00 8.78 62176 CD1 TYR A 273 21.708 76.144 35.110 1.00 11.52 6 2177 CD2 TYR A 27321.054 77.630 33.363 1.00 9.55 6 2178 CE1 TYR A 273 21.663 75.071 34.2181.00 9.62 6 2179 CE2 TYR A 273 21.087 76.577 32.482 1.00 8.45 6 2180 CZTYR A 273 21.366 75.301 32.885 1.00 10.47 6 2181 OH TYR A 273 21.36574.258 31.956 1.00 11.35 8 2182 N ALA A 274 20.678 77.001 38.308 1.0010.68 7 2183 CA ALA A 274 20.449 75.697 39.008 1.00 10.66 6 2184 C ALA A274 19.062 75.725 39.677 1.00 10.79 6 2185 O ALA A 274 18.478 74.64939.796 1.00 11.53 8 2186 CB ALA A 274 21.539 75.560 40.092 1.00 12.82 62187 N ASN A 275 18.692 76.887 40.217 1.00 11.15 7 2188 CA ASN A 27517.443 76.882 40.998 1.00 11.26 6 2189 C ASN A 275 16.199 77.051 40.1311.00 10.88 6 2190 O ASN A 275 15.082 76.705 40.606 1.00 11.83 8 2191 CBASN A 275 17.490 78.056 42.004 1.00 11.31 6 2192 CG ASN A 275 18.49577.768 43.107 1.00 11.97 6 2193 OD1 ASN A 275 18.987 76.661 43.214 1.0012.55 8 2194 ND2 ASN A 275 18.759 78.816 43.934 1.00 12.55 7 2195 N ASNA 276 16.322 77.453 38.842 1.00 11.20 7 2196 CA ASN A 276 15.129 77.70538.045 1.00 12.25 6 2197 C ASN A 276 15.023 76.992 36.720 1.00 14.18 62198 O ASN A 276 13.932 76.820 36.165 1.00 11.89 8 2199 CB ASN A 27615.134 79.197 37.632 1.00 9.94 6 2200 CG ASN A 276 14.629 80.023 38.8061.00 14.75 6 2201 OD1 ASN A 276 13.365 80.089 38.826 1.00 16.83 8 2202ND2 ASN A 276 15.551 80.529 39.612 1.00 16.12 7 2203 N SER A 277 16.15176.504 36.173 1.00 10.52 7 2204 CA SER A 277 16.064 75.974 34.811 1.0011.82 6 2205 C SER A 277 15.497 74.585 34.678 1.00 11.16 6 2206 O SER A277 15.204 74.178 33.545 1.00 12.16 8 2207 CB SER A 277 17.502 75.91134.204 1.00 11.66 6 2208 OG SER A 277 18.257 74.877 34.872 1.00 12.14 82209 N GLY A 278 15.371 73.851 35.795 1.00 11.36 7 2210 CA GLY A 27815.051 72.411 35.697 1.00 11.40 6 2211 C GLY A 278 16.263 71.565 35.3751.00 11.97 6 2212 O GLY A 278 16.115 70.348 35.279 1.00 13.61 8 2213 NVAL A 279 17.442 72.180 35.342 1.00 12.14 7 2214 CA VAL A 279 18.67371.427 35.090 1.00 10.48 6 2215 C VAL A 279 19.552 71.645 36.348 1.0011.31 6 2216 O VAL A 279 19.814 72.782 36.732 1.00 12.60 8 2217 CB VAL A279 19.362 71.989 33.830 1.00 11.56 6 2218 CG1 VAL A 279 20.628 71.19133.543 1.00 10.87 6 2219 CG2 VAL A 279 18.429 71.824 32.592 1.00 13.38 62220 N ASN A 280 20.053 70.556 36.919 1.00 10.03 7 2221 CA ASN A 28020.918 70.714 38.122 1.00 10.49 6 2222 C ASN A 280 22.294 71.095 37.5721.00 13.05 6 2223 O ASN A 280 22.506 71.116 36.365 1.00 12.57 8 2224 CBASN A 280 20.968 69.368 38.864 1.00 11.26 6 2225 CG ASN A 280 19.49269.056 39.263 1.00 9.85 6 2226 OD1 ASN A 280 18.839 69.805 39.990 1.0010.91 8 2227 ND2 ASN A 280 18.974 67.913 38.787 1.00 10.65 7 2228 N VALA 281 23.262 71.312 38.492 1.00 11.45 7 2229 CA VAL A 281 24.622 71.62137.977 1.00 9.71 6 2230 C VAL A 281 25.671 70.782 38.660 1.00 11.24 62231 O VAL A 281 25.581 70.318 39.799 1.00 11.15 8 2232 CB VAL A 28125.013 73.104 38.187 1.00 9.82 6 2233 CG1 VAL A 281 24.019 74.024 37.3971.00 10.47 6 2234 CG2 VAL A 281 25.038 73.569 39.638 1.00 11.52 6 2235 NLEU A 282 26.786 70.675 37.904 1.00 9.31 7 2236 CA LEU A 282 28.03170.087 38.460 1.00 10.27 6 2237 C LEU A 282 28.631 71.063 39.476 1.0011.17 6 2238 O LEU A 282 28.577 72.295 39.298 1.00 12.65 8 2239 CB LEU A282 29.022 69.883 37.283 1.00 10.13 6 2240 CG LEU A 282 28.650 68.55836.538 1.00 11.97 6 2241 CD1 LEU A 282 29.159 68.726 35.102 1.00 16.51 62242 CD2 LEU A 282 29.314 67.351 37.196 1.00 12.93 6 2243 N ASP A 28329.128 70.458 40.581 1.00 9.33 7 2244 CA ASP A 283 29.503 71.304 41.7641.00 11.76 6 2245 C ASP A 283 30.935 71.778 41.696 1.00 11.31 6 2246 OASP A 283 31.877 71.275 42.316 1.00 11.22 8 2247 CB ASP A 283 29.21270.451 43.014 1.00 8.73 6 2248 CG ASP A 283 29.282 71.343 44.271 1.0011.60 6 2249 OD1 ASP A 283 29.655 72.526 44.259 1.00 10.06 8 2250 OD2ASP A 283 28.866 70.758 45.290 1.00 11.95 8 2251 N PHE A 284 31.10872.815 40.834 1.00 10.41 7 2252 CA PHE A 284 32.439 73.424 40.731 1.0010.33 6 2253 C PHE A 284 32.746 74.271 41.966 1.00 11.21 6 2254 O PHE A284 33.941 74.331 42.313 1.00 12.52 8 2255 CB PHE A 284 32.509 74.40939.517 1.00 10.51 6 2256 CG PHE A 284 32.750 73.575 38.227 1.00 10.01 62257 CD1 PHE A 284 31.725 72.991 37.520 1.00 11.07 6 2258 CD2 PHE A 28434.073 73.416 37.765 1.00 11.57 6 2259 CE1 PHE A 284 31.925 72.23236.386 1.00 12.29 6 2260 CE2 PHE A 284 34.292 72.665 36.596 1.00 11.45 62261 CZ PHE A 284 33.234 72.085 35.903 1.00 9.72 6 2262 N ASP A 28531.729 74.753 42.687 1.00 9.13 7 2263 CA ASP A 285 32.061 75.575 43.8821.00 10.61 6 2264 C ASP A 285 32.799 74.670 44.885 1.00 10.95 6 2265 OASP A 285 33.806 75.092 45.468 1.00 11.00 8 2266 CB ASP A 285 30.77376.068 44.545 1.00 9.55 6 2267 CG ASP A 285 29.979 77.042 43.692 1.0010.92 6 2268 OD1 ASP A 285 30.499 77.631 42.710 1.00 12.04 8 2269 OD2ASP A 285 28.773 77.214 44.043 1.00 12.59 8 2270 N LEU A 286 32.24873.464 45.128 1.00 10.30 7 2271 CA LEU A 286 32.959 72.569 46.061 1.009.08 6 2272 C LEU A 286 34.219 71.940 45.505 1.00 9.26 6 2273 O LEU A286 35.179 71.757 46.238 1.00 11.04 8 2274 CB LEU A 286 31.968 71.41946.481 1.00 9.12 6 2275 CG LEU A 286 32.367 70.697 47.790 1.00 10.68 62276 CD1 LEU A 286 32.357 71.580 49.023 1.00 15.93 6 2277 CD2 LEU A 28631.384 69.510 47.999 1.00 13.68 6 2278 N ASN A 287 34.226 71.683 44.1681.00 9.32 7 2279 CA ASN A 287 35.441 71.091 43.586 1.00 10.65 6 2280 CASN A 287 36.687 71.937 43.872 1.00 9.75 6 2281 O ASN A 287 37.75171.401 44.184 1.00 10.35 8 2282 CB ASN A 287 35.269 71.000 42.039 1.008.74 6 2283 CG ASN A 287 36.571 70.507 41.392 1.00 11.79 6 2284 OD1 ASNA 287 37.171 71.318 40.654 1.00 11.65 8 2285 ND2 ASN A 287 36.866 69.24541.597 1.00 9.92 7 2286 N THR A 288 36.588 73.275 43.719 1.00 9.52 72287 CA THR A 288 37.769 74.106 43.907 1.00 11.58 6 2288 C THR A 28838.367 73.906 45.292 1.00 10.74 6 2289 O THR A 288 39.593 73.741 45.4861.00 13.25 8 2290 CB THR A 288 37.365 75.596 43.745 1.00 15.82 6 2291OG1 THR A 288 36.906 75.753 42.397 1.00 16.55 8 2292 CG2 THR A 28838.641 76.459 43.984 1.00 14.43 6 2293 N VAL A 289 37.440 73.847 46.2681.00 8.64 7 2294 CA VAL A 289 37.915 73.732 47.655 1.00 8.82 6 2295 CVAL A 289 38.401 72.341 47.985 1.00 11.04 6 2296 O VAL A 289 39.43872.184 48.642 1.00 11.67 8 2297 CB VAL A 289 36.780 74.237 48.605 1.0011.02 6 2298 CG1 VAL A 289 37.297 74.258 50.051 1.00 10.38 6 2299 CG2VAL A 289 36.323 75.632 48.191 1.00 11.61 6 2300 N ILE A 290 37.76471.287 47.430 1.00 9.86 7 2301 CA ILE A 290 38.262 69.911 47.642 1.008.30 6 2302 C ILE A 290 39.715 69.830 47.144 1.00 12.22 6 2303 O ILE A290 40.554 69.251 47.806 1.00 10.89 8 2304 CB ILE A 290 37.342 68.97946.851 1.00 9.93 6 2305 CG1 ILE A 290 36.004 68.833 47.591 1.00 11.46 62306 CG2 ILE A 290 38.025 67.579 46.690 1.00 11.35 6 2307 CD1 ILE A 29034.964 68.108 46.700 1.00 11.71 6 2308 N ARG A 291 39.969 70.386 45.9401.00 11.21 7 2309 CA ARG A 291 41.352 70.246 45.455 1.00 10.67 6 2310 CARG A 291 42.343 71.071 46.293 1.00 9.59 6 2311 O ARG A 291 43.48170.627 46.380 1.00 12.39 8 2312 CB ARG A 291 41.308 70.770 43.991 1.0010.96 6 2313 CG ARG A 291 40.602 69.717 43.110 1.00 11.39 6 2314 CD ARGA 291 40.480 70.173 41.647 1.00 11.11 6 2315 NE ARG A 291 41.729 70.34340.907 1.00 11.15 7 2316 CZ ARG A 291 42.225 69.361 40.109 1.00 12.12 62317 NH1 ARG A 291 41.706 68.126 40.068 1.00 11.32 7 2318 NH2 ARG A 29143.322 69.593 39.363 1.00 12.38 7 2319 N ASN A 292 41.972 72.204 46.8011.00 12.65 7 2320 CA ASN A 292 42.894 73.001 47.653 1.00 11.32 6 2321 CASN A 292 42.983 72.376 49.051 1.00 11.68 6 2322 O ASN A 292 44.07472.565 49.634 1.00 11.50 8 2323 CB ASN A 292 42.408 74.471 47.750 1.0011.01 6 2324 CG ASN A 292 42.593 75.238 46.379 1.00 14.57 6 2325 OD1 ASNA 292 43.466 74.831 45.665 1.00 19.84 8 2326 ND2 ASN A 292 41.735 76.24246.267 1.00 18.55 7 2327 N VAL A 293 42.009 71.574 49.542 1.00 10.40 72328 CA VAL A 293 42.157 71.075 50.940 1.00 10.24 6 2329 C VAL A 29342.861 69.743 50.969 1.00 11.21 6 2330 O VAL A 293 43.748 69.520 51.7831.00 11.98 8 2331 CB VAL A 293 40.703 70.961 51.499 1.00 10.95 6 2332CG1 VAL A 293 40.707 70.175 52.820 1.00 12.97 6 2333 CG2 VAL A 29340.153 72.364 51.736 1.00 13.88 6 2334 N PHE A 294 42.479 68.858 50.0331.00 11.12 7 2335 CA PHE A 294 43.106 67.537 49.960 1.00 11.38 6 2336 CPHE A 294 44.255 67.464 48.964 1.00 11.51 6 2337 O PHE A 294 45.09566.540 49.093 1.00 11.86 8 2338 CB PHE A 294 42.063 66.455 49.553 1.0011.70 6 2339 CG PHE A 294 40.936 66.334 50.584 1.00 11.57 6 2340 CD1 PHEA 294 41.178 65.683 51.808 1.00 11.48 6 2341 CD2 PHE A 294 39.707 66.86550.295 1.00 13.60 6 2342 CE1 PHE A 294 40.133 65.579 52.724 1.00 12.41 62343 CE2 PHE A 294 38.662 66.762 51.232 1.00 13.36 6 2344 CZ PHE A 29438.880 66.104 52.463 1.00 13.22 6 2345 N GLY A 295 44.295 68.355 47.9761.00 11.76 7 2346 CA GLY A 295 45.328 68.234 46.907 1.00 12.36 6 2347 CGLY A 295 46.504 69.187 47.187 1.00 10.85 6 2348 O GLY A 295 47.54768.676 47.612 1.00 13.29 8 2349 N THR A 296 46.271 70.499 46.990 1.0010.00 7 2350 CA THR A 296 47.441 71.394 47.123 1.00 11.19 6 2351 C THR A296 47.675 71.894 48.549 1.00 13.50 6 2352 O THR A 296 48.755 72.43648.874 1.00 12.22 8 2353 CB THR A 296 47.162 72.647 46.253 1.00 11.65 62354 OG1 THR A 296 46.005 73.276 46.812 1.00 15.42 8 2355 CG2 THR A 29646.976 72.308 44.770 1.00 13.16 6 2356 N PHE A 297 46.760 71.647 49.4721.00 11.24 7 2357 CA PHE A 297 46.917 72.026 50.881 1.00 12.10 6 2358 CPHE A 297 47.104 73.543 50.984 1.00 17.18 6 2359 O PHE A 297 47.71974.035 51.952 1.00 17.61 8 2360 CB PHE A 297 48.052 71.271 51.610 1.0011.80 6 2361 CG PHE A 297 47.630 69.924 52.199 1.00 14.38 6 2362 CD1 PHEA 297 47.153 68.917 51.385 1.00 13.09 6 2363 CD2 PHE A 297 47.760 69.71153.565 1.00 11.70 6 2364 CE1 PHE A 297 46.821 67.656 51.854 1.00 12.95 62365 CE2 PHE A 297 47.438 68.444 54.064 1.00 12.92 6 2366 CZ PHE A 29746.948 67.450 53.231 1.00 11.87 6 2367 N THR A 298 46.411 74.322 50.1831.00 13.51 7 2368 CA THR A 298 46.398 75.773 50.270 1.00 13.52 6 2369 CTHR A 298 45.131 76.303 50.925 1.00 13.29 6 2370 O THR A 298 45.01877.505 51.220 1.00 15.14 8 2371 CB THR A 298 46.488 76.437 48.870 1.0013.68 6 2372 OG1 THR A 298 45.446 75.982 48.035 1.00 12.95 8 2373 CG2THR A 298 47.869 76.059 48.250 1.00 15.45 6 2374 N GLN A 299 44.16275.400 51.194 1.00 10.17 7 2375 CA GLN A 299 43.009 75.785 51.975 1.0013.00 6 2376 C GLN A 299 42.852 74.738 53.114 1.00 14.72 6 2377 O GLN A299 43.624 73.753 53.094 1.00 14.92 8 2378 CB GLN A 299 41.654 75.80851.214 1.00 11.79 6 2379 CG GLN A 299 41.692 77.072 50.299 1.00 14.80 62380 CD GLN A 299 40.301 77.320 49.668 1.00 16.23 6 2381 OE1 GLN A 29939.959 76.525 48.827 1.00 15.11 8 2382 NE2 GLN A 299 39.635 78.37650.107 1.00 17.75 7 2383 N THR A 300 42.031 75.020 54.106 1.00 13.71 72384 CA THR A 300 41.924 74.106 55.252 1.00 11.61 6 2385 C THR A 30040.518 73.485 55.355 1.00 14.08 6 2386 O THR A 300 39.580 73.874 54.6441.00 11.91 8 2387 CB THR A 300 42.152 74.850 56.601 1.00 15.34 6 2388OG1 THR A 300 41.116 75.771 56.804 1.00 15.70 8 2389 CG2 THR A 30043.511 75.587 56.464 1.00 16.98 6 2390 N MET A 301 40.337 72.672 56.4431.00 11.88 7 2391 CA MET A 301 38.977 72.123 56.650 1.00 12.22 6 2392 CMET A 301 37.972 73.216 56.994 1.00 12.44 6 2393 O MET A 301 36.79173.075 56.691 1.00 11.03 8 2394 CB MET A 301 38.935 71.065 57.800 1.0012.80 6 2395 CG MET A 301 39.707 69.787 57.393 1.00 11.05 6 2396 SD META 301 39.027 69.014 55.895 1.00 12.28 16 2397 CE MET A 301 39.724 67.36656.047 1.00 14.34 6 2398 N TYR A 302 38.408 74.374 57.555 1.00 12.00 72399 CA TYR A 302 37.462 75.453 57.759 1.00 10.79 6 2400 C TYR A 30236.898 75.974 56.430 1.00 11.89 6 2401 O TYR A 302 35.694 76.181 56.3251.00 12.65 8 2402 CB TYR A 302 38.131 76.626 58.505 1.00 10.20 6 2403 CGTYR A 302 38.409 76.271 59.983 1.00 11.51 6 2404 CD1 TYR A 302 37.37576.197 60.914 1.00 16.19 6 2405 CD2 TYR A 302 39.739 76.057 60.344 1.0017.97 6 2406 CE1 TYR A 302 37.736 75.884 62.236 1.00 18.06 6 2407 CE2TYR A 302 40.062 75.723 61.683 1.00 15.93 6 2408 CZ TYR A 302 39.02975.670 62.567 1.00 19.00 6 2409 OH TYR A 302 39.409 75.355 63.905 1.0021.46 8 2410 N ASP A 303 37.763 76.026 55.418 1.00 13.06 7 2411 CA ASP A303 37.256 76.434 54.104 1.00 12.54 6 2412 C ASP A 303 36.285 75.40953.492 1.00 11.88 6 2413 O ASP A 303 35.330 75.782 52.785 1.00 13.46 82414 CB ASP A 303 38.419 76.666 53.133 1.00 10.93 6 2415 CG ASP A 30339.386 77.734 53.654 1.00 14.78 6 2416 OD1 ASP A 303 38.879 78.87753.849 1.00 13.77 8 2417 OD2 ASP A 303 40.573 77.435 53.832 1.00 13.10 82418 N LEU A 304 36.602 74.152 53.720 1.00 11.36 7 2419 CA LEU A 30435.713 73.086 53.156 1.00 11.06 6 2420 C LEU A 304 34.348 73.181 53.8411.00 12.95 6 2421 O LEU A 304 33.315 73.111 53.155 1.00 11.60 8 2422 CBLEU A 304 36.393 71.742 53.367 1.00 10.48 6 2423 CG LEU A 304 35.68770.566 52.633 1.00 11.09 6 2424 CD1 LEU A 304 35.737 70.797 51.112 1.0012.57 6 2425 CD2 LEU A 304 36.397 69.248 52.971 1.00 12.54 6 2426 N ASNA 305 34.290 73.255 55.180 1.00 11.76 7 2427 CA ASN A 305 32.999 73.42255.887 1.00 12.74 6 2428 C ASN A 305 32.308 74.720 55.479 1.00 11.54 62429 O ASN A 305 31.100 74.673 55.259 1.00 13.50 8 2430 CB ASN A 30533.331 73.448 57.405 1.00 12.22 6 2431 CG ASN A 305 32.014 73.551 58.2101.00 12.84 6 2432 OD1 ASN A 305 31.174 72.669 58.097 1.00 13.98 8 2433ND2 ASN A 305 31.910 74.651 58.967 1.00 17.24 7 2434 N ASN A 306 33.06175.772 55.272 1.00 11.86 7 2435 CA ASN A 306 32.418 77.036 54.848 1.0012.68 6 2436 C ASN A 306 31.740 76.830 53.499 1.00 13.44 6 2437 O ASN A306 30.672 77.409 53.225 1.00 13.40 8 2438 CB ASN A 306 33.438 78.17654.774 1.00 12.13 6 2439 CG ASN A 306 33.863 78.686 56.143 1.00 20.79 62440 OD1 ASN A 306 33.275 78.499 57.233 1.00 23.19 8 2441 ND2 ASN A 30634.959 79.477 56.155 1.00 24.17 7 2442 N MET A 307 32.405 76.105 52.5891.00 11.55 7 2443 CA MET A 307 31.750 75.915 51.254 1.00 11.38 6 2444 CMET A 307 30.590 74.957 51.272 1.00 12.48 6 2445 O MET A 307 29.63975.156 50.512 1.00 13.10 8 2446 CB MET A 307 32.849 75.431 50.252 1.0012.11 6 2447 CG MET A 307 32.375 75.462 48.767 1.00 12.14 6 2448 SD META 307 31.759 77.075 48.246 1.00 12.77 16 2449 CE MET A 307 33.282 78.01048.324 1.00 13.86 6 2450 N VAL A 308 30.592 73.951 52.152 1.00 10.38 72451 CA VAL A 308 29.383 73.136 52.340 1.00 10.10 6 2452 C VAL A 30828.272 74.049 52.822 1.00 11.64 6 2453 O VAL A 308 27.153 73.974 52.3211.00 13.14 8 2454 CB VAL A 308 29.712 72.052 53.406 1.00 13.16 6 2455CG1 VAL A 308 28.388 71.356 53.770 1.00 14.05 6 2456 CG2 VAL A 30830.641 71.038 52.727 1.00 13.08 6 2457 N ASN A 309 28.541 74.952 53.7841.00 12.04 7 2458 CA ASN A 309 27.479 75.848 54.264 1.00 12.56 6 2459 CASN A 309 27.073 76.824 53.176 1.00 13.56 6 2460 O ASN A 309 25.87577.017 53.030 1.00 15.38 8 2461 CB ASN A 309 27.997 76.680 55.470 1.0014.00 6 2462 CG ASN A 309 28.109 75.761 56.684 1.00 20.56 6 2463 OD1 ASNA 309 27.432 74.725 56.748 1.00 26.71 8 2464 ND2 ASN A 309 28.967 76.20857.595 1.00 21.18 7 2465 N GLN A 310 27.970 77.423 52.426 1.00 14.28 72466 CA GLN A 310 27.549 78.422 51.422 1.00 13.95 6 2467 C GLN A 31026.734 77.754 50.319 1.00 13.50 6 2468 O GLN A 310 25.672 78.286 49.9421.00 14.03 8 2469 CB GLN A 310 28.821 79.123 50.869 1.00 14.99 6 2470 CGGLN A 310 28.507 80.214 49.859 1.00 21.08 6 2471 CD GLN A 310 29.73481.169 49.819 1.00 21.08 6 2472 OE1 GLN A 310 30.875 80.762 50.019 1.0025.61 8 2473 NE2 GLN A 310 29.417 82.401 49.600 1.00 25.23 7 2474 N THRA 311 27.238 76.630 49.792 1.00 11.65 7 2475 CA THR A 311 26.432 75.98348.711 1.00 11.52 6 2476 C THR A 311 25.089 75.459 49.257 1.00 12.57 62477 O THR A 311 24.039 75.572 48.599 1.00 13.81 8 2478 CB THR A 31127.143 74.754 48.142 1.00 12.52 6 2479 OG1 THR A 311 27.593 73.90949.194 1.00 13.67 8 2480 CG2 THR A 311 28.426 75.250 47.375 1.00 14.32 62481 N GLY A 312 25.096 75.107 50.561 1.00 11.69 7 2482 CA GLY A 31223.812 74.642 51.137 1.00 14.78 6 2483 C GLY A 312 22.800 75.792 51.2231.00 14.32 6 2484 O GLY A 312 21.573 75.473 51.276 1.00 16.33 8 2485 NASN A 313 23.320 76.998 51.476 1.00 13.08 7 2486 CA ASN A 313 22.39278.108 51.535 1.00 13.20 6 2487 C ASN A 313 21.980 78.575 50.150 1.0014.89 6 2488 O ASN A 313 20.827 79.097 50.014 1.00 20.75 8 2489 CB ASN A313 23.155 79.260 52.204 1.00 19.18 6 2490 CG ASN A 313 23.210 79.02453.718 1.00 30.91 6 2491 OD1 ASN A 313 22.384 78.310 54.281 1.00 30.04 82492 ND2 ASN A 313 24.152 79.691 54.360 1.00 31.03 7 2493 N GLU A 31422.802 78.394 49.111 1.00 12.83 7 2494 CA GLU A 314 22.396 79.060 47.8221.00 11.95 6 2495 C GLU A 314 21.621 78.137 46.889 1.00 13.20 6 2496 OGLU A 314 20.733 78.689 46.175 1.00 13.02 8 2497 CB GLU A 314 23.75379.394 47.117 1.00 10.17 6 2498 CG GLU A 314 24.503 80.510 47.842 1.0012.02 6 2499 CD GLU A 314 25.715 80.987 46.985 1.00 15.94 6 2500 OE1 GLUA 314 26.285 80.206 46.232 1.00 15.22 8 2501 OE2 GLU A 314 26.164 82.10047.284 1.00 24.00 8 2502 N TYR A 315 21.992 76.840 46.892 1.00 11.76 72503 CA TYR A 315 21.297 75.979 45.885 1.00 10.85 6 2504 C TYR A 31520.032 75.368 46.506 1.00 12.73 6 2505 O TYR A 315 20.140 74.648 47.5101.00 12.47 8 2506 CB TYR A 315 22.265 74.838 45.494 1.00 12.39 6 2507 CGTYR A 315 23.437 75.394 44.699 1.00 10.41 6 2508 CD1 TYR A 315 23.27075.610 43.316 1.00 11.23 6 2509 CD2 TYR A 315 24.613 75.785 45.297 1.0012.52 6 2510 CE1 TYR A 315 24.333 76.166 42.586 1.00 12.92 6 2511 CE2TYR A 315 25.686 76.350 44.563 1.00 10.90 6 2512 CZ TYR A 315 25.51076.507 43.187 1.00 12.76 6 2513 OH TYR A 315 26.595 77.056 42.517 1.0013.74 8 2514 N LYS A 316 18.895 75.634 45.861 1.00 11.54 7 2515 CA LYS A316 17.638 75.080 46.395 1.00 14.39 6 2516 C LYS A 316 17.578 73.55546.454 1.00 15.27 6 2517 O LYS A 316 17.175 72.963 47.475 1.00 14.60 82518 CB LYS A 316 16.496 75.595 45.485 1.00 14.77 6 2519 CG LYS A 31615.139 75.068 46.091 1.00 18.12 6 2520 CD LYS A 316 13.982 75.856 45.5651.00 22.24 6 2521 CE LYS A 316 12.683 75.166 46.061 1.00 19.23 6 2522 NZLYS A 316 12.432 75.635 47.468 1.00 22.20 7 2523 N TYR A 317 18.22772.953 45.457 1.00 13.10 7 2524 CA TYR A 317 18.316 71.483 45.445 1.0011.39 6 2525 C TYR A 317 19.805 71.123 45.506 1.00 10.31 6 2526 O TYR A317 20.410 70.491 44.637 1.00 12.52 8 2527 CB TYR A 317 17.652 70.89344.157 1.00 12.53 6 2528 CG TYR A 317 16.221 71.387 44.004 1.00 13.61 62529 CD1 TYR A 317 15.272 70.932 44.915 1.00 14.65 6 2530 CD2 TYR A 31715.800 72.280 43.030 1.00 14.34 6 2531 CE1 TYR A 317 13.938 71.36644.811 1.00 13.78 6 2532 CE2 TYR A 317 14.511 72.767 42.890 1.00 12.10 62533 CZ TYR A 317 13.604 72.246 43.832 1.00 15.19 6 2534 OH TYR A 31712.275 72.682 43.733 1.00 14.53 8 2535 N LYS A 318 20.375 71.463 46.7021.00 11.46 7 2536 CA LYS A 318 21.821 71.130 46.865 1.00 10.64 6 2537 CLYS A 318 22.053 69.651 46.865 1.00 10.21 6 2538 O LYS A 318 23.13369.145 46.529 1.00 10.36 8 2539 CB LYS A 318 22.408 71.772 48.141 1.009.85 6 2540 CG LYS A 318 21.843 71.211 49.451 1.00 13.57 6 2541 CD LYS A318 20.619 72.105 49.820 1.00 19.29 6 2542 CE LYS A 318 20.309 72.06451.345 1.00 19.13 6 2543 NZ LYS A 318 19.066 72.819 51.636 1.00 20.57 72544 N GLU A 319 21.044 68.796 47.174 1.00 9.32 7 2545 CA GLU A 31921.217 67.359 47.096 1.00 11.07 6 2546 C GLU A 319 21.164 66.802 45.6671.00 12.26 6 2547 O GLU A 319 21.469 65.627 45.504 1.00 11.85 8 2548 CBGLU A 319 20.021 66.636 47.827 1.00 12.74 6 2549 CG GLU A 319 19.99867.027 49.320 1.00 15.35 6 2550 CD GLU A 319 19.346 68.353 49.656 1.0019.53 6 2551 OE1 GLU A 319 18.645 68.996 48.818 1.00 14.20 8 2552 OE2GLU A 319 19.503 68.829 50.839 1.00 14.17 8 2553 N ASN A 320 21.03367.681 44.664 1.00 9.38 7 2554 CA ASN A 320 21.155 67.324 43.285 1.009.77 6 2555 C ASN A 320 22.454 67.819 42.636 1.00 12.36 6 2556 O ASN A320 22.736 67.591 41.442 1.00 10.93 8 2557 CB ASN A 320 19.995 67.90142.402 1.00 10.57 6 2558 CG ASN A 320 18.660 67.290 42.784 1.00 14.03 62559 OD1 ASN A 320 18.619 66.275 43.445 1.00 13.17 8 2560 ND2 ASN A 32017.558 67.901 42.323 1.00 10.64 7 2561 N LEU A 321 23.285 68.499 43.4221.00 10.68 7 2562 CA LEU A 321 24.610 68.918 42.896 1.00 10.60 6 2563 CLEU A 321 25.415 67.643 42.685 1.00 10.70 6 2564 O LEU A 321 25.44866.685 43.452 1.00 11.96 8 2565 CB LEU A 321 25.299 69.733 44.024 1.009.53 6 2566 CG LEU A 321 24.761 71.176 44.124 1.00 9.68 6 2567 CD1 LEU A321 25.310 71.820 45.415 1.00 13.05 6 2568 CD2 LEU A 321 25.183 72.06442.930 1.00 9.85 6 2569 N ILE A 322 26.185 67.671 41.566 1.00 9.04 72570 CA ILE A 322 27.014 66.478 41.265 1.00 9.68 6 2571 C ILE A 32228.477 66.821 41.584 1.00 11.13 6 2572 O ILE A 322 29.071 67.716 40.9351.00 10.40 8 2573 CB ILE A 322 26.872 66.118 39.767 1.00 10.10 6 2574CG1 ILE A 322 25.387 65.842 39.384 1.00 9.96 6 2575 CG2 ILE A 322 27.79364.954 39.396 1.00 12.80 6 2576 CD1 ILE A 322 24.773 64.698 40.258 1.009.05 6 2577 N THR A 323 29.019 66.133 42.594 1.00 9.87 7 2578 CA THR A323 30.333 66.524 43.130 1.00 8.82 6 2579 C THR A 323 31.433 65.70442.453 1.00 9.73 6 2580 O THR A 323 31.218 64.628 41.902 1.00 10.64 82581 CB THR A 323 30.364 66.302 44.652 1.00 10.77 6 2582 OG1 THR A 32330.009 64.919 44.887 1.00 10.73 8 2583 CG2 THR A 323 29.314 67.23745.318 1.00 10.06 6 2584 N PHE A 324 32.660 66.234 42.559 1.00 9.44 72585 CA PHE A 324 33.784 65.582 41.880 1.00 10.80 6 2586 C PHE A 32435.086 66.205 42.385 1.00 9.58 6 2587 O PHE A 324 35.086 67.375 42.8051.00 10.73 8 2588 CB PHE A 324 33.716 65.698 40.286 1.00 9.57 6 2589 CGPHE A 324 33.638 67.122 39.817 1.00 9.02 6 2590 CD1 PHE A 324 32.42167.817 39.810 1.00 11.94 6 2591 CD2 PHE A 324 34.798 67.746 39.354 1.0011.07 6 2592 CE1 PHE A 324 32.321 69.142 39.380 1.00 11.10 6 2593 CE2PHE A 324 34.683 69.083 38.926 1.00 11.33 6 2594 CZ PHE A 324 33.49869.788 38.931 1.00 13.68 6 2595 N ILE A 325 36.137 65.385 42.285 1.009.28 7 2596 CA ILE A 325 37.469 65.879 42.710 1.00 9.24 6 2597 C ILE A325 38.277 66.277 41.480 1.00 9.67 6 2598 O ILE A 325 39.255 67.11641.645 1.00 10.76 8 2599 CB AILE A 325 38.211 64.869 43.596 0.60 11.75 62600 CG1 AILE A 325 38.779 63.705 42.764 0.60 10.90 6 2601 CG2 AILE A325 37.288 64.325 44.695 0.60 12.60 6 2602 CD1 AILE A 325 39.550 62.69343.585 0.60 10.36 6 2599 CB BILE A 325 38.139 64.627 43.330 0.40 12.90 62600 CG1 BILE A 325 37.386 64.127 44.568 0.40 10.36 6 2601 CG2 BILE A325 39.604 64.862 43.640 0.40 10.82 6 2602 CD1 BILE A 325 37.571 62.65144.847 0.40 13.69 6 2603 N ASP A 326 38.028 65.680 40.350 1.00 9.63 72604 CA ASP A 326 38.762 65.987 39.107 1.00 10.15 6 2605 C ASP A 32637.813 65.625 37.964 1.00 11.71 6 2606 O ASP A 326 36.678 65.102 38.2091.00 10.86 8 2607 CB ASP A 326 40.149 65.323 39.050 1.00 12.00 6 2608 CGASP A 326 40.166 63.807 39.089 1.00 12.49 6 2609 OD1 ASP A 326 39.08063.207 38.870 1.00 12.13 8 2610 OD2 ASP A 326 41.228 63.200 39.354 1.0011.72 8 2611 N ASN A 327 38.279 65.749 36.731 1.00 9.05 7 2612 CA ASN A327 37.486 65.359 35.569 1.00 10.52 6 2613 C ASN A 327 38.334 65.55634.352 1.00 9.98 6 2614 O ASN A 327 39.573 65.686 34.478 1.00 11.19 82615 CB ASN A 327 36.177 66.162 35.432 1.00 11.56 6 2616 CG ASN A 32736.351 67.636 35.121 1.00 12.65 6 2617 OD1 ASN A 327 37.355 68.10634.634 1.00 11.48 8 2618 ND2 ASN A 327 35.314 68.376 35.463 1.00 8.99 72619 N HIS A 328 37.802 65.385 33.178 1.00 9.23 7 2620 CA HIS A 32838.599 65.393 31.958 1.00 11.14 6 2621 C HIS A 328 39.037 66.779 31.4711.00 11.62 6 2622 O HIS A 328 39.744 66.836 30.450 1.00 11.55 8 2623 CBHIS A 328 37.726 64.740 30.844 1.00 10.61 6 2624 CG HIS A 328 36.51165.577 30.526 1.00 9.76 6 2625 ND1 HIS A 328 35.652 65.938 31.572 1.0011.58 7 2626 CD2 HIS A 328 36.012 66.093 29.370 1.00 11.35 6 2627 CE1HIS A 328 34.648 66.668 31.066 1.00 12.44 6 2628 NE2 HIS A 328 34.85366.756 29.733 1.00 11.88 7 2629 N ASP A 329 38.746 67.808 32.263 1.008.48 7 2630 CA ASP A 329 39.181 69.155 31.893 1.00 9.03 6 2631 C ASP A329 40.073 69.793 32.960 1.00 12.15 6 2632 O ASP A 329 40.388 71.01232.883 1.00 12.94 8 2633 CB ASP A 329 37.955 70.091 31.837 1.00 11.03 62634 CG ASP A 329 37.069 69.815 30.620 1.00 11.95 6 2635 OD1 ASP A 32937.477 69.188 29.617 1.00 11.39 8 2636 OD2 ASP A 329 35.891 70.24330.712 1.00 11.11 8 2637 N MET A 330 40.568 68.936 33.857 1.00 11.19 72638 CA MET A 330 41.533 69.433 34.857 1.00 9.36 6 2639 C MET A 33042.537 68.330 35.211 1.00 9.51 6 2640 O MET A 330 42.224 67.156 34.9271.00 11.47 8 2641 CB MET A 330 40.858 70.015 36.111 1.00 13.17 6 2642 CGMET A 330 40.005 68.973 36.857 1.00 11.23 6 2643 SD MET A 330 39.08769.743 38.236 1.00 12.96 16 2644 CE MET A 330 37.923 70.706 37.364 1.0013.78 6 2645 N SER A 331 43.702 68.680 35.765 1.00 10.04 7 2646 CA SER A331 44.650 67.618 36.030 1.00 9.86 6 2647 C SER A 331 44.130 66.55737.020 1.00 11.24 6 2648 O SER A 331 43.295 66.892 37.858 1.00 11.71 82649 CB SER A 331 46.009 68.207 36.629 1.00 11.21 6 2650 OG SER A 33145.623 68.981 37.793 1.00 14.33 8 2651 N ARG A 332 44.540 65.321 36.8331.00 11.49 7 2652 CA ARG A 332 44.057 64.272 37.749 1.00 11.49 6 2653 CARG A 332 44.499 64.603 39.189 1.00 11.63 6 2654 O ARG A 332 45.59165.103 39.412 1.00 12.21 8 2655 CB ARG A 332 44.667 62.914 37.387 1.0013.45 6 2656 CG ARG A 332 43.997 62.516 36.049 1.00 16.61 6 2657 CD ARGA 332 43.560 61.101 36.061 1.00 20.26 6 2658 NE ARG A 332 43.017 60.59234.777 1.00 15.50 7 2659 CZ ARG A 332 41.965 59.753 34.882 1.00 12.48 62660 NH1 ARG A 332 41.546 59.388 36.094 1.00 10.61 7 2661 NH2 ARG A 33241.440 59.251 33.741 1.00 10.74 7 2662 N PHE A 333 43.654 64.168 40.1531.00 9.55 7 2663 CA PHE A 333 44.019 64.431 41.533 1.00 10.54 6 2664 CPHE A 333 45.461 63.976 41.852 1.00 12.40 6 2665 O PHE A 333 46.17064.709 42.515 1.00 13.01 8 2666 CB PHE A 333 43.007 63.676 42.481 1.0011.67 6 2667 CG PHE A 333 43.365 64.006 43.958 1.00 12.76 6 2668 CD1 PHEA 333 44.315 63.230 44.587 1.00 15.62 6 2669 CD2 PHE A 333 42.718 65.04144.556 1.00 18.86 6 2670 CE1 PHE A 333 44.651 63.513 45.905 1.00 19.61 62671 CE2 PHE A 333 43.014 65.342 45.906 1.00 15.77 6 2672 CZ PHE A 33343.978 64.561 46.492 1.00 16.46 6 2673 N LEU A 334 45.825 62.763 41.4621.00 10.49 7 2674 CA LEU A 334 47.183 62.257 41.835 1.00 14.60 6 2675 CLEU A 334 48.303 63.035 41.167 1.00 12.74 6 2676 O LEU A 334 49.45662.864 41.627 1.00 13.05 8 2677 CB LEU A 334 47.269 60.748 41.476 1.0013.94 6 2678 CG LEU A 334 46.461 59.910 42.484 1.00 13.29 6 2679 CD1 LEUA 334 46.488 58.447 41.969 1.00 14.98 6 2680 CD2 LEU A 334 47.045 59.90543.909 1.00 13.51 6 2681 N SER A 335 48.014 63.857 40.144 1.00 11.98 72682 CA SER A 335 49.117 64.732 39.639 1.00 11.30 6 2683 C SER A 33549.115 66.026 40.421 1.00 15.22 6 2684 O SER A 335 50.159 66.664 40.4381.00 18.21 8 2685 CB SER A 335 48.843 65.113 38.179 1.00 14.88 6 2686 OGSER A 335 49.221 63.920 37.436 1.00 17.27 8 2687 N VAL A 336 48.04166.315 41.169 1.00 11.92 7 2688 CA VAL A 336 48.092 67.455 42.094 1.0014.73 6 2689 C VAL A 336 48.805 67.064 43.392 1.00 15.20 6 2690 O VAL A336 49.593 67.825 43.962 1.00 16.13 8 2691 CB VAL A 336 46.691 67.97042.447 1.00 14.37 6 2692 CG1 VAL A 336 46.646 69.120 43.441 1.00 16.05 62693 CG2 VAL A 336 45.970 68.386 41.154 1.00 18.05 6 2694 N ASN A 33748.525 65.866 43.852 1.00 13.19 7 2695 CA ASN A 337 49.114 65.389 45.1321.00 12.41 6 2696 C ASN A 337 49.153 63.870 44.976 1.00 12.10 6 2697 OASN A 337 48.082 63.178 44.865 1.00 11.76 8 2698 CB ASN A 337 48.14165.756 46.272 1.00 11.12 6 2699 CG ASN A 337 48.570 65.206 47.621 1.0013.14 6 2700 OD1 ASN A 337 49.572 64.466 47.738 1.00 12.58 8 2701 ND2ASN A 337 47.865 65.514 48.694 1.00 11.19 7 2702 N SER A 338 50.36463.275 44.939 1.00 9.71 7 2703 CA SER A 338 50.477 61.849 44.747 1.0013.36 6 2704 C SER A 338 50.257 60.983 45.993 1.00 11.43 6 2705 O SER A338 50.294 59.759 45.858 1.00 14.29 8 2706 CB SER A 338 51.884 61.46144.225 1.00 17.19 6 2707 OG SER A 338 52.871 61.883 45.154 1.00 17.12 82708 N ASN A 339 49.847 61.610 47.095 1.00 13.33 7 2709 CA ASN A 33949.601 60.788 48.297 1.00 12.26 6 2710 C ASN A 339 48.267 60.043 48.1931.00 12.82 6 2711 O ASN A 339 47.246 60.732 48.134 1.00 12.55 8 2712 CBASN A 339 49.554 61.769 49.485 1.00 10.37 6 2713 CG ASN A 339 49.51660.949 50.787 1.00 18.65 6 2714 OD1 ASN A 339 48.403 60.509 51.110 1.0019.28 8 2715 ND2 ASN A 339 50.648 60.809 51.502 1.00 18.28 7 2716 N LYSA 340 48.283 58.708 48.148 1.00 12.73 7 2717 CA LYS A 340 47.008 58.02147.941 1.00 11.20 6 2718 C LYS A 340 46.077 58.134 49.122 1.00 13.56 62719 O LYS A 340 44.859 58.103 48.906 1.00 12.11 8 2720 CB LYS A 34047.345 56.523 47.665 1.00 12.59 6 2721 CG LYS A 340 48.006 56.401 46.2791.00 12.90 6 2722 CD LYS A 340 48.318 54.903 46.055 1.00 18.47 6 2723 CELYS A 340 48.937 54.658 44.699 1.00 18.65 6 2724 NZ LYS A 340 50.37755.099 44.564 1.00 22.63 7 2725 N ALA A 341 46.585 58.363 50.345 1.0012.85 7 2726 CA ALA A 341 45.626 58.557 51.453 1.00 14.45 6 2727 C ALA A341 44.835 59.830 51.239 1.00 13.48 6 2728 O ALA A 341 43.661 59.85551.568 1.00 11.31 8 2729 CB ALA A 341 46.346 58.628 52.806 1.00 15.23 62730 N ASN A 342 45.459 60.911 50.731 1.00 10.37 7 2731 CA ASN A 34244.717 62.126 50.470 1.00 10.38 6 2732 C ASN A 342 43.687 61.897 49.3591.00 10.62 6 2733 O ASN A 342 42.560 62.477 49.439 1.00 12.01 8 2734 CBASN A 342 45.708 63.276 50.141 1.00 11.46 6 2735 CG ASN A 342 46.51963.737 51.351 1.00 13.17 6 2736 OD1 ASN A 342 47.710 64.044 51.127 1.0012.82 8 2737 ND2 ASN A 342 45.888 63.859 52.516 1.00 12.05 7 2738 N LEUA 343 44.001 61.049 48.344 1.00 10.66 7 2739 CA LEU A 343 42.953 60.71547.377 1.00 10.18 6 2740 C LEU A 343 41.810 59.935 48.039 1.00 12.28 62741 O LEU A 343 40.635 60.288 47.781 1.00 11.44 8 2742 CB LEU A 34343.581 59.854 46.229 1.00 10.02 6 2743 CG LEU A 343 42.546 59.182 45.2951.00 10.27 6 2744 CD1 LEU A 343 41.847 60.288 44.550 1.00 13.59 6 2745CD2 LEU A 343 43.309 58.294 44.283 1.00 12.64 6 2746 N HIS A 344 42.17358.977 48.898 1.00 11.47 7 2747 CA HIS A 344 41.093 58.185 49.570 1.0011.49 6 2748 C HIS A 344 40.189 59.122 50.370 1.00 13.40 6 2749 O HIS A344 38.951 58.916 50.500 1.00 12.11 8 2750 CB HIS A 344 41.731 57.07550.439 1.00 9.09 6 2751 CG HIS A 344 42.520 56.064 49.656 1.00 10.04 62752 ND1 HIS A 344 43.612 55.436 50.199 1.00 12.75 7 2753 CD2 HIS A 34442.363 55.580 48.370 1.00 11.63 6 2754 CE1 HIS A 344 44.114 54.61249.289 1.00 10.72 6 2755 NE2 HIS A 344 43.393 54.662 48.157 1.00 12.61 72756 N GLN A 345 40.834 60.100 51.024 1.00 10.53 7 2757 CA GLN A 34540.049 61.036 51.831 1.00 10.43 6 2758 C GLN A 345 39.077 61.899 51.0081.00 10.42 6 2759 O GLN A 345 37.888 62.067 51.324 1.00 10.38 8 2760 CBGLN A 345 40.996 62.012 52.564 1.00 11.01 6 2761 CG GLN A 345 41.84761.258 53.641 1.00 9.73 6 2762 CD GLN A 345 43.142 62.041 53.786 1.0010.78 6 2763 OE1 GLN A 345 43.232 63.196 53.279 1.00 12.69 8 2764 NE2GLN A 345 44.170 61.448 54.428 1.00 12.87 7 2765 N ALA A 346 39.59062.418 49.883 1.00 11.81 7 2766 CA ALA A 346 38.762 63.250 48.987 1.0010.44 6 2767 C ALA A 346 37.604 62.379 48.462 1.00 11.17 6 2768 O ALA A346 36.473 62.887 48.339 1.00 11.30 8 2769 CB ALA A 346 39.595 63.82747.829 1.00 9.34 6 2770 N LEU A 347 37.895 61.107 48.079 1.00 12.34 72771 CA LEU A 347 36.809 60.261 47.589 1.00 11.12 6 2772 C LEU A 34735.777 59.999 48.733 1.00 9.98 6 2773 O LEU A 347 34.567 60.087 48.4661.00 11.63 8 2774 CB LEU A 347 37.367 58.885 47.187 1.00 11.26 6 2775 CGLEU A 347 38.146 58.913 45.840 1.00 14.75 6 2776 CD1 LEU A 347 38.82957.574 45.530 1.00 13.09 6 2777 CD2 LEU A 347 37.132 59.197 44.722 1.0015.41 6 2778 N ALA A 348 36.304 59.764 49.955 1.00 10.14 7 2779 CA ALA A348 35.269 59.479 51.003 1.00 10.67 6 2780 C ALA A 348 34.432 60.72551.273 1.00 12.22 6 2781 O ALA A 348 33.231 60.600 51.534 1.00 11.88 82782 CB ALA A 348 36.008 59.130 52.310 1.00 10.16 6 2783 N PHE A 34935.026 61.922 51.160 1.00 10.08 7 2784 CA PHE A 349 34.258 63.149 51.3301.00 10.26 6 2785 C PHE A 349 33.120 63.213 50.282 1.00 9.67 6 2786 OPHE A 349 31.942 63.422 50.717 1.00 11.25 8 2787 CB PHE A 349 35.27064.348 51.200 1.00 9.92 6 2788 CG PHE A 349 34.515 65.659 51.357 1.008.60 6 2789 CD1 PHE A 349 34.016 66.030 52.605 1.00 11.80 6 2790 CD2 PHEA 349 34.340 66.526 50.249 1.00 11.51 6 2791 CE1 PHE A 349 33.296 67.24752.714 1.00 11.90 6 2792 CE2 PHE A 349 33.638 67.709 50.409 1.00 10.49 62793 CZ PHE A 349 33.069 68.068 51.660 1.00 12.88 6 2794 N ILE A 35033.411 63.030 49.005 1.00 8.49 7 2795 CA ILE A 350 32.257 63.124 48.0891.00 10.97 6 2796 C ILE A 350 31.361 61.899 48.158 1.00 11.48 6 2797 OILE A 350 30.139 62.115 47.958 1.00 11.30 8 2798 CB ILE A 350 32.67663.380 46.605 1.00 11.26 6 2799 CG1 ILE A 350 33.451 62.279 45.983 1.0011.16 6 2800 CG2 ILE A 350 33.429 64.742 46.556 1.00 12.07 6 2801 CD1ILE A 350 33.748 62.454 44.463 1.00 9.59 6 2802 N LEU A 351 31.87360.731 48.548 1.00 9.78 7 2803 CA LEU A 351 30.930 59.601 48.655 1.009.90 6 2804 C LEU A 351 29.956 59.782 49.809 1.00 11.10 6 2805 O LEU A351 28.888 59.122 49.698 1.00 11.60 8 2806 CB LEU A 351 31.813 58.34948.879 1.00 11.35 6 2807 CG LEU A 351 32.492 57.907 47.564 1.00 10.64 62808 CD1 LEU A 351 33.679 56.944 47.822 1.00 12.51 6 2809 CD2 LEU A 35131.500 57.262 46.595 1.00 13.68 6 2810 N THR A 352 30.267 60.590 50.8501.00 9.74 7 2811 CA THR A 352 29.310 60.657 51.960 1.00 11.34 6 2812 CTHR A 352 28.658 62.022 52.149 1.00 12.86 6 2813 O THR A 352 27.82262.214 53.022 1.00 13.09 8 2814 CB THR A 352 30.099 60.375 53.296 1.0011.44 6 2815 OG1 THR A 352 31.244 61.234 53.420 1.00 11.08 8 2816 CG2THR A 352 30.607 58.939 53.324 1.00 9.52 6 2817 N SER A 353 29.10063.028 51.368 1.00 10.03 7 2818 CA SER A 353 28.530 64.357 51.432 1.0010.73 6 2819 C SER A 353 27.299 64.574 50.536 1.00 9.28 6 2820 O SER A353 26.990 63.688 49.726 1.00 13.31 8 2821 CB SER A 353 29.607 65.40351.012 1.00 12.91 6 2822 OG SER A 353 30.626 65.402 52.045 1.00 12.40 82823 N ARG A 354 26.646 65.741 50.754 1.00 10.25 7 2824 CA ARG A 35425.379 65.920 50.024 1.00 10.03 6 2825 C ARG A 354 25.611 65.997 48.5331.00 10.84 6 2826 O ARG A 354 26.704 66.369 48.085 1.00 11.59 8 2827 CBARG A 354 24.669 67.185 50.545 1.00 10.71 6 2828 CG ARG A 354 25.09968.504 49.838 1.00 11.61 6 2829 CD ARG A 354 26.535 68.853 50.229 1.0012.49 6 2830 NE ARG A 354 26.964 70.130 49.548 1.00 12.69 7 2831 CZ ARGA 354 27.455 70.157 48.317 1.00 12.54 6 2832 NH1 ARG A 354 27.638 69.11347.497 1.00 12.15 7 2833 NH2 ARG A 354 27.867 71.370 47.894 1.00 11.14 72834 N GLY A 355 24.542 65.707 47.780 1.00 11.00 7 2835 CA GLY A 35524.624 65.584 46.318 1.00 10.49 6 2836 C GLY A 355 25.149 64.196 45.9291.00 13.18 6 2837 O GLY A 355 25.154 63.299 46.788 1.00 15.74 8 2838 NTHR A 356 25.546 64.007 44.688 1.00 10.24 7 2839 CA THR A 356 25.88562.648 44.202 1.00 10.01 6 2840 C THR A 356 27.279 62.722 43.581 1.0010.67 6 2841 O THR A 356 27.512 63.621 42.769 1.00 10.61 8 2842 CB THR A356 24.908 62.301 43.066 1.00 13.21 6 2843 OG1 THR A 356 23.622 62.05243.698 1.00 11.93 8 2844 CG2 THR A 356 25.332 60.948 42.433 1.00 11.53 62845 N PRO A 357 28.184 61.868 43.967 1.00 10.42 7 2846 CA PRO A 35729.564 61.929 43.493 1.00 10.52 6 2847 C PRO A 357 29.689 61.366 42.0921.00 11.14 6 2848 O PRO A 357 29.074 60.379 41.752 1.00 11.48 8 2849 CBPRO A 357 30.340 61.021 44.494 1.00 10.57 6 2850 CG PRO A 357 29.24559.991 44.834 1.00 11.58 6 2851 CD PRO A 357 27.914 60.760 44.914 1.0010.88 6 2852 N SER A 358 30.508 62.051 41.293 1.00 8.23 7 2853 CA SER A358 31.003 61.558 40.001 1.00 9.73 6 2854 C SER A 358 32.509 61.27240.069 1.00 10.56 6 2855 O SER A 358 33.323 62.183 40.331 1.00 11.97 82856 CB SER A 358 30.768 62.634 38.921 1.00 12.36 6 2857 OG SER A 35831.301 62.159 37.653 1.00 13.42 8 2858 N ILE A 359 32.813 59.992 39.9151.00 9.37 7 2859 CA ILE A 359 34.234 59.557 39.927 1.00 9.47 6 2860 CILE A 359 34.703 59.350 38.492 1.00 12.04 6 2861 O ILE A 359 34.10158.730 37.647 1.00 11.59 8 2862 CB ILE A 359 34.313 58.205 40.671 1.0011.89 6 2863 CG1 ILE A 359 33.858 58.478 42.145 1.00 14.90 6 2864 CG2ILE A 359 35.727 57.624 40.550 1.00 12.39 6 2865 CD1 ILE A 359 33.93657.155 42.925 1.00 22.17 6 2866 N TYR A 360 35.810 60.088 38.176 1.009.52 7 2867 CA TYR A 360 36.364 60.076 36.807 1.00 8.41 6 2868 C TYR A360 37.027 58.709 36.636 1.00 9.86 6 2869 O TYR A 360 37.780 58.22737.510 1.00 10.81 8 2870 CB TYR A 360 37.399 61.247 36.796 1.00 9.51 62871 CG TYR A 360 37.935 61.510 35.363 1.00 9.64 6 2872 CD1 TYR A 36037.191 61.428 34.206 1.00 10.11 6 2873 CD2 TYR A 360 39.279 61.88235.294 1.00 9.54 6 2874 CE1 TYR A 360 37.818 61.650 32.960 1.00 10.79 62875 CE2 TYR A 360 39.927 62.148 34.066 1.00 10.73 6 2876 CZ TYR A 36039.153 62.044 32.937 1.00 11.36 6 2877 OH TYR A 360 39.712 62.217 31.6701.00 10.12 8 2878 N TYR A 361 36.808 58.146 35.418 1.00 10.09 7 2879 CATYR A 361 37.279 56.773 35.210 1.00 10.66 6 2880 C TYR A 361 38.74856.616 35.593 1.00 11.54 6 2881 O TYR A 361 39.556 57.488 35.297 1.0011.37 8 2882 CB TYR A 361 37.051 56.287 33.730 1.00 9.71 6 2883 CG TYR A361 38.086 56.846 32.765 1.00 10.50 6 2884 CD1 TYR A 361 37.937 58.15032.332 1.00 10.91 6 2885 CD2 TYR A 361 39.176 56.052 32.383 1.00 10.62 62886 CE1 TYR A 361 38.913 58.715 31.480 1.00 10.92 6 2887 CE2 TYR A 36140.155 56.601 31.520 1.00 9.87 6 2888 CZ TYR A 361 39.988 57.930 31.1391.00 12.35 6 2889 OH TYR A 361 40.982 58.482 30.297 1.00 11.60 8 2890 NGLY A 362 39.069 55.475 36.171 1.00 11.61 7 2891 CA GLY A 362 40.45455.099 36.513 1.00 12.01 6 2892 C GLY A 362 40.997 55.744 37.772 1.0011.04 6 2893 O GLY A 362 42.168 55.431 38.093 1.00 12.36 8 2894 N THR A363 40.222 56.614 38.446 1.00 12.35 7 2895 CA THR A 363 40.676 57.16939.736 1.00 11.24 6 2896 C THR A 363 41.033 56.009 40.693 1.00 11.33 62897 O THR A 363 42.072 56.074 41.376 1.00 12.29 8 2898 CB THR A 36339.528 57.957 40.387 1.00 11.07 6 2899 OG1 THR A 363 39.248 59.06539.494 1.00 12.04 8 2900 CG2 THR A 363 40.024 58.554 41.730 1.00 11.22 62901 N GLU A 364 40.221 54.961 40.670 1.00 11.97 7 2902 CA GLU A 36440.379 53.835 41.610 1.00 11.29 6 2903 C GLU A 364 41.520 52.938 41.1981.00 12.77 6 2904 O GLU A 364 41.845 51.968 41.915 1.00 14.39 8 2905 CBGLU A 364 38.994 53.093 41.712 1.00 10.27 6 2906 CG GLU A 364 38.65252.265 40.469 1.00 11.76 6 2907 CD GLU A 364 38.139 53.001 39.248 1.0015.28 6 2908 OE1 GLU A 364 38.072 54.257 39.239 1.00 13.43 8 2909 OE2GLU A 364 37.813 52.343 38.247 1.00 11.75 8 2910 N GLN A 365 42.04653.105 39.993 1.00 10.80 7 2911 CA GLN A 365 43.256 52.398 39.542 1.0011.28 6 2912 C GLN A 365 44.462 53.305 39.629 1.00 12.82 6 2913 O GLN A365 45.606 52.953 39.219 1.00 12.70 8 2914 CB GLN A 365 43.138 51.92338.088 1.00 12.65 6 2915 CG GLN A 365 41.964 50.951 37.828 1.00 9.91 62916 CD GLN A 365 42.043 49.690 38.693 1.00 14.70 6 2917 OE1 GLN A 36541.016 49.200 39.269 1.00 17.54 8 2918 NE2 GLN A 365 43.204 49.14238.847 1.00 12.05 7 2919 N TYR A 366 44.317 54.426 40.333 1.00 10.84 72920 CA TYR A 366 45.443 55.357 40.582 1.00 10.38 6 2921 C TYR A 36646.039 55.921 39.308 1.00 13.18 6 2922 O TYR A 366 47.248 56.182 39.2051.00 14.90 8 2923 CB TYR A 366 46.547 54.753 41.514 1.00 11.57 6 2924 CGTYR A 366 45.872 54.326 42.813 1.00 11.25 6 2925 CD1 TYR A 366 45.27055.215 43.707 1.00 14.66 6 2926 CD2 TYR A 366 45.942 52.977 43.139 1.0013.34 6 2927 CE1 TYR A 366 44.653 54.747 44.882 1.00 15.95 6 2928 CE2TYR A 366 45.361 52.494 44.332 1.00 14.89 6 2929 CZ TYR A 366 44.71153.395 45.154 1.00 12.93 6 2930 OH TYR A 366 44.118 52.939 46.302 1.0012.26 8 2931 N MET A 367 45.147 56.315 38.357 1.00 12.15 7 2932 CA MET A367 45.700 56.998 37.181 1.00 10.89 6 2933 C MET A 367 46.195 58.36537.586 1.00 14.58 6 2934 O MET A 367 45.501 59.019 38.383 1.00 14.18 82935 CB MET A 367 44.602 57.163 36.115 1.00 11.31 6 2936 CG MET A 36744.316 55.810 35.397 1.00 11.19 6 2937 SD MET A 367 42.994 56.012 34.1391.00 13.40 16 2938 CE MET A 367 43.986 56.859 32.873 1.00 13.82 6 2939 NALA A 368 47.271 58.817 36.904 1.00 12.72 7 2940 CA ALA A 368 47.68960.193 37.152 1.00 14.30 6 2941 C ALA A 368 47.745 60.849 35.754 1.0014.06 6 2942 O ALA A 368 47.702 60.187 34.694 1.00 19.49 8 2943 CB ALA A368 49.047 60.184 37.904 1.00 15.40 6 2944 N GLY A 369 47.908 62.15235.729 1.00 14.57 7 2945 CA GLY A 369 48.101 62.780 34.408 1.00 15.04 62946 C GLY A 369 47.715 64.242 34.571 1.00 16.47 6 2947 O GLY A 36946.895 64.643 35.433 1.00 13.93 8 2948 N GLY A 370 48.524 65.045 33.8721.00 12.36 7 2949 CA GLY A 370 48.282 66.487 33.864 1.00 15.60 6 2950 CGLY A 370 47.034 66.898 33.102 1.00 14.31 6 2951 O GLY A 370 46.20266.015 32.888 1.00 18.42 8 2952 N ASN A 371 46.994 68.167 32.710 1.0014.57 7 2953 CA ASN A 371 45.708 68.579 32.081 1.00 14.92 6 2954 C ASN A371 45.594 68.064 30.645 1.00 14.23 6 2955 O ASN A 371 46.556 67.57030.084 1.00 14.23 8 2956 CB AASN A 371 45.420 70.051 32.240 0.60 23.78 62957 CG AASN A 371 43.956 70.451 32.279 0.60 25.40 6 2958 OD1 AASN A 37143.002 69.778 31.899 0.60 11.28 8 2959 ND2 AASN A 371 43.728 71.69532.756 0.60 26.08 7 2956 CB BASN A 371 45.872 70.115 31.871 0.40 16.79 62957 CG BASN A 371 44.590 70.670 32.513 0.40 29.87 6 2958 OD1 BASN A 37143.560 70.829 31.849 0.40 28.56 8 2959 ND2 BASN A 371 44.801 70.90933.793 0.40 23.38 7 2960 N ASP A 372 44.373 68.230 30.152 1.00 12.86 72961 CA ASP A 372 44.018 67.780 28.792 1.00 12.97 6 2962 C ASP A 37245.054 67.942 27.745 1.00 12.07 6 2963 O ASP A 372 45.503 69.093 27.6141.00 13.32 8 2964 CB ASP A 372 42.737 68.624 28.451 1.00 10.31 6 2965 CGASP A 372 42.153 68.351 27.084 1.00 11.02 6 2966 OD1 ASP A 372 42.55667.384 26.464 1.00 12.81 8 2967 OD2 ASP A 372 41.293 69.190 26.659 1.0012.58 8 2968 N PRO A 373 45.561 66.874 27.151 1.00 11.77 7 2969 CA PRO A373 44.932 65.582 26.928 1.00 11.70 6 2970 C PRO A 373 45.436 64.54427.918 1.00 11.76 6 2971 O PRO A 373 45.014 63.392 27.879 1.00 11.30 82972 CB PRO A 373 45.237 65.136 25.475 1.00 10.91 6 2973 CG PRO A 37346.632 65.755 25.353 1.00 14.12 6 2974 CD PRO A 373 46.484 67.082 26.0401.00 13.69 6 2975 N TYR A 374 46.374 64.933 28.815 1.00 9.68 7 2976 CATYR A 374 47.139 63.921 29.579 1.00 10.60 6 2977 C TYR A 374 46.38163.338 30.741 1.00 11.01 6 2978 O TYR A 374 46.896 62.356 31.346 1.0012.41 8 2979 CB TYR A 374 48.493 64.515 30.101 1.00 12.69 6 2980 CG TYRA 374 49.258 65.009 28.884 1.00 14.15 6 2981 CD1 TYR A 374 49.738 64.10727.954 1.00 14.25 6 2982 CD2 TYR A 374 49.457 66.382 28.664 1.00 19.98 62983 CE1 TYR A 374 50.385 64.536 26.798 1.00 19.01 6 2984 CE2 TYR A 37450.125 66.791 27.525 1.00 18.34 6 2985 CZ TYR A 374 50.572 65.893 26.6131.00 21.81 6 2986 OH TYR A 374 51.271 66.349 25.492 1.00 24.57 8 2987 NASN A 375 45.203 63.895 31.004 1.00 10.61 7 2988 CA ASN A 375 44.29563.320 31.991 1.00 9.59 6 2989 C ASN A 375 43.275 62.353 31.357 1.0011.84 6 2990 O ASN A 375 42.406 61.795 32.073 1.00 12.18 8 2991 CB ASN A375 43.489 64.456 32.649 1.00 10.84 6 2992 CG ASN A 375 42.822 65.35631.632 1.00 13.47 6 2993 OD1 ASN A 375 42.889 65.147 30.378 1.00 14.66 82994 ND2 ASN A 375 42.188 66.403 32.155 1.00 11.13 7 2995 N ARG A 37643.519 62.009 30.071 1.00 11.23 7 2996 CA ARG A 376 42.622 61.074 29.3661.00 12.81 6 2997 C ARG A 376 43.410 59.886 28.872 1.00 11.47 6 2998 OARG A 376 43.286 59.389 27.744 1.00 11.36 8 2999 CB ARG A 376 41.97561.789 28.128 1.00 11.93 6 3000 CG ARG A 376 41.111 62.997 28.659 1.0011.44 6 3001 CD ARG A 376 40.908 63.980 27.521 1.00 13.66 6 3002 NE ARGA 376 40.177 65.214 28.005 1.00 13.05 7 3003 CZ ARG A 376 39.567 66.01127.137 1.00 11.35 6 3004 NH1 ARG A 376 39.569 65.752 25.825 1.00 9.57 73005 NH2 ARG A 376 38.944 67.071 27.646 1.00 10.95 7 3006 N GLY A 37744.270 59.361 29.749 1.00 9.89 7 3007 CA GLY A 377 45.084 58.173 29.4071.00 10.61 6 3008 C GLY A 377 44.162 56.943 29.297 1.00 11.99 6 3009 OGLY A 377 42.974 56.949 29.658 1.00 10.52 8 3010 N MET A 378 44.78355.861 28.718 1.00 12.46 7 3011 CA MET A 378 43.968 54.622 28.638 1.0011.69 6 3012 C MET A 378 43.777 54.021 30.032 1.00 11.73 6 3013 O MET A378 44.769 53.836 30.804 1.00 12.80 8 3014 CB MET A 378 44.714 53.60627.749 1.00 13.64 6 3015 CG MET A 378 43.750 52.572 27.113 1.00 12.65 63016 SD MET A 378 42.871 53.357 25.713 1.00 14.01 16 3017 CE MET A 37841.543 52.139 25.530 1.00 15.94 6 3018 N MET A 379 42.575 53.515 30.3241.00 11.68 7 3019 CA MET A 379 42.364 52.843 31.637 1.00 11.67 6 3020 CMET A 379 43.364 51.711 31.705 1.00 14.11 6 3021 O MET A 379 43.46350.864 30.812 1.00 12.85 8 3022 CB MET A 379 40.896 52.323 31.558 1.0012.77 6 3023 CG MET A 379 40.572 51.443 32.790 1.00 13.09 6 3024 SD META 379 40.355 52.467 34.277 1.00 13.28 16 3025 CE MET A 379 39.369 51.26935.254 1.00 13.26 6 3026 N PRO A 380 44.193 51.636 32.750 1.00 12.95 73027 CA PRO A 380 45.398 50.827 32.726 1.00 14.01 6 3028 C PRO A 38045.170 49.402 33.204 1.00 17.99 6 3029 O PRO A 380 46.005 48.554 32.9141.00 17.24 8 3030 CB PRO A 380 46.384 51.501 33.699 1.00 14.68 6 3031 CGPRO A 380 45.418 52.190 34.636 1.00 16.71 6 3032 CD PRO A 380 44.30052.693 33.751 1.00 14.00 6 3033 N ALA A 381 44.099 49.232 33.975 1.0015.78 7 3034 CA ALA A 381 43.895 47.955 34.625 1.00 13.86 6 3035 C ALA A381 42.477 47.891 35.190 1.00 13.98 6 3036 O ALA A 381 41.859 48.95235.215 1.00 13.69 8 3037 CB ALA A 381 44.854 47.608 35.761 1.00 17.52 63038 N PHE A 382 42.029 46.671 35.497 1.00 14.05 7 3039 CA PHE A 38240.701 46.466 36.094 1.00 12.60 6 3040 C PHE A 382 40.791 45.644 37.3931.00 12.68 6 3041 O PHE A 382 39.963 44.765 37.641 1.00 15.80 8 3042 CBPHE A 382 39.742 45.806 35.052 1.00 15.36 6 3043 CG PHE A 382 39.61946.669 33.826 1.00 14.57 6 3044 CD1 PHE A 382 40.475 46.629 32.737 1.0014.43 6 3045 CD2 PHE A 382 38.572 47.618 33.775 1.00 16.09 6 3046 CE1PHE A 382 40.327 47.480 31.670 1.00 17.87 6 3047 CE2 PHE A 382 38.41448.469 32.699 1.00 12.38 6 3048 CZ PHE A 382 39.293 48.395 31.613 1.0015.80 6 3049 N ASP A 383 41.721 46.138 38.224 1.00 13.84 7 3050 CA ASP A383 42.065 45.402 39.467 1.00 15.38 6 3051 C ASP A 383 41.067 45.73240.552 1.00 15.05 6 3052 O ASP A 383 40.864 46.868 40.943 1.00 16.64 83053 CB ASP A 383 43.457 45.826 39.901 1.00 13.18 6 3054 CG ASP A 38344.015 45.155 41.165 1.00 18.89 6 3055 OD1 ASP A 383 43.286 44.42841.805 1.00 20.99 8 3056 OD2 ASP A 383 45.229 45.408 41.363 1.00 21.43 83057 N THR A 384 40.302 44.680 40.950 1.00 13.75 7 3058 CA THR A 38439.215 44.894 41.930 1.00 12.49 6 3059 C THR A 384 39.773 44.871 43.3451.00 13.78 6 3060 O THR A 384 38.951 44.852 44.298 1.00 18.13 8 3061 CBTHR A 384 38.098 43.831 41.755 1.00 16.42 6 3062 OG1 THR A 384 38.72542.525 41.937 1.00 18.75 8 3063 CG2 THR A 384 37.515 43.943 40.342 1.0020.28 6 3064 N THR A 385 41.088 44.832 43.573 1.00 14.37 7 3065 CA THR A385 41.648 44.691 44.906 1.00 16.71 6 3066 C THR A 385 42.313 45.97445.424 1.00 16.63 6 3067 O THR A 385 42.873 45.952 46.539 1.00 14.22 83068 CB THR A 385 42.693 43.546 45.009 1.00 19.15 6 3069 OG1 THR A 38543.883 43.878 44.288 1.00 17.99 8 3070 CG2 THR A 385 42.075 42.23444.541 1.00 24.33 6 3071 N THR A 386 42.254 47.039 44.606 1.00 14.92 73072 CA THR A 386 42.952 48.254 45.131 1.00 13.63 6 3073 C THR A 38642.175 48.801 46.328 1.00 11.22 6 3074 O THR A 386 40.990 48.649 46.4781.00 12.74 8 3075 CB THR A 386 43.101 49.344 44.054 1.00 13.50 6 3076OG1 THR A 386 41.805 49.919 43.822 1.00 12.14 8 3077 CG2 THR A 38643.656 48.809 42.719 1.00 17.62 6 3078 N THR A 387 42.886 49.552 47.1841.00 14.21 7 3079 CA THR A 387 42.237 50.167 48.316 1.00 11.44 6 3080 CTHR A 387 41.127 51.134 47.887 1.00 12.54 6 3081 O THR A 387 40.04551.113 48.437 1.00 12.57 8 3082 CB THR A 387 43.277 50.926 49.145 1.0017.16 6 3083 OG1 THR A 387 44.177 49.939 49.669 1.00 15.42 8 3084 CG2THR A 387 42.644 51.724 50.273 1.00 14.27 6 3085 N ALA A 388 41.44151.910 46.838 1.00 13.30 7 3086 CA ALA A 388 40.376 52.785 46.360 1.0010.83 6 3087 C ALA A 388 39.162 52.083 45.808 1.00 12.23 6 3088 O ALA A388 38.030 52.497 46.001 1.00 11.44 8 3089 CB ALA A 388 40.968 53.70045.239 1.00 10.26 6 3090 N PHE A 389 39.347 50.956 45.084 1.00 12.53 73091 CA PHE A 389 38.202 50.182 44.579 1.00 13.64 6 3092 C PHE A 38937.361 49.746 45.779 1.00 13.47 6 3093 O PHE A 389 36.157 49.895 45.7891.00 12.37 8 3094 CB PHE A 389 38.766 48.975 43.763 1.00 11.46 6 3095 CGPHE A 389 37.627 48.178 43.141 1.00 12.01 6 3096 CD1 PHE A 389 36.93647.248 43.916 1.00 16.87 6 3097 CD2 PHE A 389 37.375 48.299 41.777 1.0014.39 6 3098 CE1 PHE A 389 35.869 46.515 43.383 1.00 14.50 6 3099 CE2PHE A 389 36.340 47.536 41.216 1.00 12.44 6 3100 CZ PHE A 389 35.64646.648 42.031 1.00 13.69 6 3101 N LYS A 390 38.053 49.160 46.775 1.0012.03 7 3102 CA LYS A 390 37.303 48.672 47.936 1.00 12.63 6 3103 C LYS A390 36.544 49.767 48.699 1.00 14.75 6 3104 O LYS A 390 35.438 49.55649.197 1.00 12.66 8 3105 CB LYS A 390 38.291 48.000 48.917 1.00 12.06 63106 CG LYS A 390 38.798 46.712 48.243 1.00 15.90 6 3107 CD LYS A 39039.589 45.970 49.325 1.00 25.81 6 3108 CE LYS A 390 40.980 46.524 49.4401.00 29.79 6 3109 NZ LYS A 390 41.835 45.465 50.107 1.00 41.01 7 3110 NGLU A 391 37.256 50.908 48.782 1.00 11.21 7 3111 CA GLU A 391 36.63652.048 49.475 1.00 11.43 6 3112 C GLU A 391 35.375 52.482 48.742 1.0012.51 6 3113 O GLU A 391 34.300 52.735 49.337 1.00 10.64 8 3114 CB GLU A391 37.670 53.223 49.487 1.00 10.44 6 3115 CG GLU A 391 36.957 54.51949.997 1.00 10.67 6 3116 CD GLU A 391 37.870 55.744 49.810 1.00 12.38 63117 OE1 GLU A 391 38.974 55.628 49.226 1.00 13.12 8 3118 OE2 GLU A 39137.458 56.841 50.284 1.00 12.94 8 3119 N VAL A 392 35.455 52.675 47.4031.00 11.36 7 3120 CA VAL A 392 34.279 53.176 46.653 1.00 12.25 6 3121 CVAL A 392 33.156 52.128 46.716 1.00 12.76 6 3122 O VAL A 392 31.96852.481 46.930 1.00 12.77 8 3123 CB VAL A 392 34.667 53.410 45.175 1.0014.39 6 3124 CG1 VAL A 392 33.434 53.661 44.296 1.00 13.75 6 3125 CG2VAL A 392 35.702 54.570 45.061 1.00 12.07 6 3126 N SER A 393 33.48750.846 46.628 1.00 10.90 7 3127 CA SER A 393 32.426 49.822 46.686 1.0012.19 6 3128 C SER A 393 31.708 49.782 48.021 1.00 10.96 6 3129 O SER A393 30.469 49.774 48.186 1.00 12.48 8 3130 CB SER A 393 33.059 48.43146.394 1.00 12.79 6 3131 OG SER A 393 31.944 47.538 46.423 1.00 19.93 83132 N THR A 394 32.493 49.942 49.099 1.00 11.04 7 3133 CA THR A 39431.920 49.922 50.445 1.00 12.34 6 3134 C THR A 394 31.061 51.130 50.6821.00 11.80 6 3135 O THR A 394 29.935 51.097 51.169 1.00 11.63 8 3136 CBTHR A 394 33.039 49.889 51.509 1.00 12.40 6 3137 OG1 THR A 394 33.69948.614 51.401 1.00 14.67 8 3138 CG2 THR A 394 32.443 50.011 52.927 1.0014.84 6 3139 N LEU A 395 31.600 52.334 50.322 1.00 12.76 7 3140 CA LEU A395 30.858 53.558 50.592 1.00 11.35 6 3141 C LEU A 395 29.666 53.70949.624 1.00 10.18 6 3142 O LEU A 395 28.676 54.373 49.976 1.00 11.69 83143 CB LEU A 395 31.784 54.804 50.604 1.00 13.30 6 3144 CG LEU A 39532.795 54.745 51.811 1.00 12.96 6 3145 CD1 LEU A 395 33.641 56.01951.748 1.00 13.55 6 3146 CD2 LEU A 395 32.059 54.747 53.145 1.00 14.45 63147 N ALA A 396 29.852 53.116 48.444 1.00 11.70 7 3148 CA ALA A 39628.636 53.182 47.557 1.00 12.78 6 3149 C ALA A 396 27.498 52.378 48.1631.00 13.72 6 3150 O ALA A 396 26.345 52.797 48.075 1.00 10.99 8 3151 CBALA A 396 29.035 52.530 46.203 1.00 12.34 6 3152 N GLY A 397 27.79751.244 48.825 1.00 11.86 7 3153 CA GLY A 397 26.710 50.490 49.510 1.0012.95 6 3154 C GLY A 397 26.096 51.295 50.656 1.00 12.93 6 3155 O GLY A397 24.865 51.276 50.842 1.00 15.22 8 3156 N LEU A 398 26.948 52.01851.404 1.00 12.12 7 3157 CA LEU A 398 26.336 52.833 52.491 1.00 10.40 63158 C LEU A 398 25.388 53.871 51.900 1.00 13.47 6 3159 O LEU A 39824.310 54.166 52.434 1.00 13.29 8 3160 CB LEU A 398 27.503 53.525 53.2291.00 10.78 6 3161 CG LEU A 398 26.999 54.426 54.353 1.00 11.76 6 3162CD1 LEU A 398 26.326 53.660 55.479 1.00 15.25 6 3163 CD2 LEU A 39828.230 55.206 54.909 1.00 16.57 6 3164 N ARG A 399 25.832 54.478 50.7541.00 11.98 7 3165 CA ARG A 399 24.988 55.539 50.164 1.00 12.52 6 3166 CARG A 399 23.712 54.952 49.579 1.00 13.24 6 3167 O ARG A 399 22.66155.603 49.688 1.00 14.42 8 3168 CB ARG A 399 25.789 56.271 49.068 1.0011.24 6 3169 CG ARG A 399 24.974 57.205 48.158 1.00 11.40 6 3170 CD ARGA 399 25.933 57.875 47.182 1.00 11.42 6 3171 NE ARG A 399 26.620 59.02947.799 1.00 10.92 7 3172 CZ ARG A 399 26.193 60.279 47.877 1.00 14.21 63173 NH1 ARG A 399 24.965 60.565 47.446 1.00 10.96 7 3174 NH2 ARG A 39926.954 61.245 48.436 1.00 11.76 7 3175 N ARG A 400 23.713 53.697 49.1311.00 12.24 7 3176 CA ARG A 400 22.456 53.111 48.675 1.00 12.96 6 3177 CARG A 400 21.533 52.789 49.852 1.00 13.71 6 3178 O ARG A 400 20.31152.762 49.629 1.00 17.33 8 3179 CB ARG A 400 22.748 51.783 47.930 1.0014.09 6 3180 CG ARG A 400 23.460 51.918 46.578 1.00 14.91 6 3181 CD ARGA 400 23.412 50.634 45.761 1.00 16.08 6 3182 NE ARG A 400 24.141 49.51746.399 1.00 14.78 7 3183 CZ ARG A 400 25.452 49.279 46.343 1.00 14.12 63184 NH1 ARG A 400 26.214 50.128 45.640 1.00 15.84 7 3185 NH2 ARG A 40025.957 48.216 46.978 1.00 16.89 7 3186 N ASN A 401 22.154 52.394 50.9721.00 14.24 7 3187 CA ASN A 401 21.271 51.879 52.060 1.00 14.18 6 3188 CASN A 401 20.967 52.828 53.189 1.00 15.56 6 3189 O ASN A 401 19.97652.564 53.935 1.00 17.91 8 3190 CB ASN A 401 21.990 50.632 52.590 1.0016.43 6 3191 CG ASN A 401 21.827 49.617 51.404 1.00 25.29 6 3192 OD1 ASNA 401 22.805 49.256 50.797 1.00 33.03 8 3193 ND2 ASN A 401 20.619 49.21551.102 1.00 40.20 7 3194 N ASN A 402 21.705 53.948 53.373 1.00 13.76 73195 CA ASN A 402 21.449 54.851 54.506 1.00 13.71 6 3196 C ASN A 40220.938 56.175 53.980 1.00 14.67 6 3197 O ASN A 402 21.601 56.923 53.2491.00 13.53 8 3198 CB ASN A 402 22.753 55.036 55.311 1.00 13.24 6 3199 CGASN A 402 22.397 55.744 56.604 1.00 14.53 6 3200 OD1 ASN A 402 21.72256.787 56.564 1.00 14.56 8 3201 ND2 ASN A 402 22.839 55.186 57.762 1.0011.48 7 3202 N ALA A 403 19.633 56.460 54.202 1.00 12.55 7 3203 CA ALA A403 19.017 57.672 53.679 1.00 12.81 6 3204 C ALA A 403 19.622 58.96154.144 1.00 14.88 6 3205 O ALA A 403 19.421 59.958 53.422 1.00 13.18 83206 CB ALA A 403 17.511 57.608 54.092 1.00 12.99 6 3207 N ALA A 40420.407 58.945 55.229 1.00 11.82 7 3208 CA ALA A 404 21.107 60.187 55.6111.00 11.98 6 3209 C ALA A 404 22.095 60.641 54.524 1.00 11.49 6 3210 OALA A 404 22.259 61.857 54.383 1.00 12.58 8 3211 CB ALA A 404 21.87460.008 56.930 1.00 15.02 6 3212 N ILE A 405 22.707 59.716 53.830 1.0011.27 7 3213 CA ILE A 405 23.702 60.168 52.791 1.00 11.62 6 3214 C ILE A405 22.936 60.722 51.581 1.00 13.21 6 3215 O ILE A 405 23.353 61.69650.964 1.00 12.14 8 3216 CB ILE A 405 24.538 58.973 52.331 1.00 14.54 63217 CG1 ILE A 405 25.425 58.253 53.392 1.00 15.40 6 3218 CG2 ILE A 40525.511 59.410 51.202 1.00 11.30 6 3219 CD1 ILE A 405 26.170 59.26654.247 1.00 17.36 6 3220 N GLN A 406 21.759 60.152 51.297 1.00 11.32 73221 CA GLN A 406 20.992 60.545 50.107 1.00 11.87 6 3222 C GLN A 40620.335 61.902 50.300 1.00 14.28 6 3223 O GLN A 406 20.265 62.707 49.3601.00 11.82 8 3224 CB GLN A 406 19.875 59.494 49.869 1.00 12.00 6 3225 CGGLN A 406 20.511 58.136 49.549 1.00 12.17 6 3226 CD GLN A 406 19.52156.983 49.392 1.00 22.22 6 3227 OE1 GLN A 406 19.847 55.775 49.395 1.0020.31 8 3228 NE2 GLN A 406 18.272 57.356 49.223 1.00 24.04 7 3229 N TYRA 407 19.757 62.154 51.499 1.00 13.05 7 3230 CA TYR A 407 18.848 63.26151.702 1.00 13.56 6 3231 C TYR A 407 19.168 64.182 52.885 1.00 10.35 63232 O TYR A 407 18.463 65.190 53.047 1.00 12.85 8 3233 CB TYR A 40717.440 62.678 52.068 1.00 14.06 6 3234 CG TYR A 407 16.935 61.567 51.1441.00 12.51 6 3235 CD1 TYR A 407 16.929 61.748 49.759 1.00 11.68 6 3236CD2 TYR A 407 16.397 60.418 51.708 1.00 11.57 6 3237 CE1 TYR A 40716.441 60.742 48.918 1.00 12.71 6 3238 CE2 TYR A 407 15.910 59.42050.894 1.00 14.60 6 3239 CZ TYR A 407 15.933 59.595 49.515 1.00 15.50 63240 OH TYR A 407 15.433 58.598 48.707 1.00 15.89 8 3241 N GLY A 40820.152 63.743 53.678 1.00 12.31 7 3242 CA GLY A 408 20.277 64.361 55.0051.00 14.17 6 3243 C GLY A 408 20.830 65.790 55.030 1.00 13.76 6 3244 OGLY A 408 21.566 66.253 54.133 1.00 13.31 8 3245 N THR A 409 20.63666.393 56.207 1.00 12.33 7 3246 CA THR A 409 21.322 67.645 56.558 1.0014.50 6 3247 C THR A 409 22.822 67.370 56.707 1.00 13.72 6 3248 O THR A409 23.222 66.229 56.777 1.00 12.71 8 3249 CB THR A 409 20.812 68.21057.928 1.00 16.13 6 3250 OG1 THR A 409 20.849 67.169 58.916 1.00 16.69 83251 CG2 THR A 409 19.360 68.677 57.762 1.00 18.70 6 3252 N THR A 41023.605 68.449 56.790 1.00 12.28 7 3253 CA THR A 410 25.062 68.261 57.1411.00 12.15 6 3254 C THR A 410 25.332 69.229 58.321 1.00 12.71 6 3255 OTHR A 410 25.041 70.423 58.225 1.00 13.99 8 3256 CB THR A 410 25.94368.740 55.952 1.00 11.34 6 3257 OG1 THR A 410 25.541 67.959 54.786 1.0013.77 8 3258 CG2 THR A 410 27.425 68.392 56.192 1.00 13.33 6 3259 N THRA 411 25.996 68.665 59.342 1.00 12.78 7 3260 CA THR A 411 26.301 69.43060.568 1.00 12.27 6 3261 C THR A 411 27.765 69.192 60.919 1.00 13.51 63262 O THR A 411 28.168 68.039 61.036 1.00 14.10 8 3263 CB THR A 41125.386 68.891 61.718 1.00 13.83 6 3264 OG1 THR A 411 24.000 69.12061.364 1.00 15.26 8 3265 CG2 THR A 411 25.620 69.676 62.991 1.00 17.79 63266 N GLN A 412 28.501 70.302 61.110 1.00 12.74 7 3267 CA GLN A 41229.899 70.153 61.592 1.00 13.61 6 3268 C GLN A 412 29.894 69.765 63.0621.00 13.43 6 3269 O GLN A 412 29.218 70.451 63.824 1.00 15.64 8 3270 CBGLN A 412 30.556 71.523 61.335 1.00 14.70 6 3271 CG GLN A 412 31.99971.615 61.876 1.00 22.99 6 3272 CD GLN A 412 31.918 72.168 63.334 1.0022.07 6 3273 OE1 GLN A 412 32.409 71.438 64.163 1.00 19.41 8 3274 NE2GLN A 412 31.358 73.310 63.633 1.00 25.10 7 3275 N ARG A 413 30.69468.721 63.330 1.00 11.94 7 3276 CA ARG A 413 30.768 68.223 64.700 1.0011.40 6 3277 C ARG A 413 32.184 68.430 65.276 1.00 12.19 6 3278 O ARG A413 32.263 68.482 66.510 1.00 12.20 8 3279 CB ARG A 413 30.356 66.75664.815 1.00 16.20 6 3280 CG ARG A 413 28.840 66.557 64.562 1.00 13.09 63281 CD ARG A 413 27.968 67.296 65.579 1.00 13.13 6 3282 NE ARG A 41326.611 66.668 65.580 1.00 14.79 7 3283 CZ ARG A 413 25.684 66.909 66.5151.00 19.43 6 3284 NH1 ARG A 413 25.974 67.784 67.503 1.00 16.73 7 3285NH2 ARG A 413 24.529 66.233 66.470 1.00 18.22 7 3286 N TRP A 414 33.22868.466 64.474 1.00 11.18 7 3287 CA TRP A 414 34.548 68.752 65.082 1.0012.61 6 3288 C TRP A 414 35.444 69.243 63.947 1.00 13.80 6 3289 O TRP A414 35.295 68.712 62.833 1.00 13.58 8 3290 CB TRP A 414 35.121 67.43865.651 1.00 14.04 6 3291 CG TRP A 414 36.181 67.603 66.709 1.00 14.49 63292 CD1 TRP A 414 35.921 67.473 68.075 1.00 15.45 6 3293 CD2 TRP A 41437.583 67.864 66.591 1.00 15.74 6 3294 NE1 TRP A 414 37.112 67.62268.773 1.00 16.17 7 3295 CE2 TRP A 414 38.123 67.884 67.898 1.00 15.43 63296 CE3 TRP A 414 38.421 68.101 65.507 1.00 14.89 6 3297 CZ2 TRP A 41439.489 68.090 68.138 1.00 20.21 6 3298 CZ3 TRP A 414 39.805 68.27965.725 1.00 15.42 6 3299 CH2 TRP A 414 40.310 68.296 67.066 1.00 17.01 63300 N ILE A 415 36.215 70.337 64.186 1.00 12.40 7 3301 CA ILE A 41537.012 70.828 63.038 1.00 11.33 6 3302 C ILE A 415 38.296 71.491 63.5241.00 15.04 6 3303 O ILE A 415 38.300 72.134 64.600 1.00 15.39 8 3304 CBILE A 415 36.153 71.827 62.253 1.00 15.29 6 3305 CG1 ILE A 415 36.84372.197 60.923 1.00 15.07 6 3306 CG2 ILE A 415 35.782 73.061 63.054 1.0020.69 6 3307 CD1 ILE A 415 35.862 72.686 59.854 1.00 18.18 6 3308 N ASNA 416 39.349 71.266 62.797 1.00 13.47 7 3309 CA ASN A 416 40.517 72.15262.912 1.00 14.63 6 3310 C ASN A 416 41.103 72.198 61.526 1.00 13.17 63311 O ASN A 416 40.399 71.879 60.536 1.00 12.76 8 3312 CB ASN A 41641.480 71.607 63.994 1.00 14.61 6 3313 CG ASN A 416 42.250 70.394 63.6691.00 16.07 6 3314 OD1 ASN A 416 42.180 69.778 62.591 1.00 12.99 8 3315ND2 ASN A 416 43.129 69.947 64.597 1.00 16.12 7 3316 N ASN A 417 42.35672.644 61.313 1.00 13.23 7 3317 CA ASN A 417 42.755 72.836 59.907 1.0013.30 6 3318 C ASN A 417 42.767 71.526 59.103 1.00 13.34 6 3319 O ASN A417 42.621 71.524 57.886 1.00 12.55 8 3320 CB ASN A 417 44.185 73.41059.931 1.00 16.87 6 3321 CG ASN A 417 44.190 74.929 59.999 1.00 23.81 63322 OD1 ASN A 417 43.170 75.585 60.178 1.00 21.65 8 3323 ND2 ASN A 41745.415 75.482 59.839 1.00 24.48 7 3324 N ASP A 418 43.109 70.439 59.8741.00 12.62 7 3325 CA ASP A 418 43.295 69.150 59.209 1.00 10.76 6 3326 CASP A 418 42.126 68.157 59.319 1.00 12.08 6 3327 O ASP A 418 42.09367.177 58.533 1.00 11.98 8 3328 CB ASP A 418 44.520 68.478 59.846 1.0013.38 6 3329 CG ASP A 418 45.842 69.080 59.483 1.00 16.78 6 3330 OD1 ASPA 418 46.040 69.609 58.372 1.00 13.55 8 3331 OD2 ASP A 418 46.759 69.01760.342 1.00 13.98 8 3332 N VAL A 419 41.304 68.369 60.363 1.00 11.52 73333 CA VAL A 419 40.281 67.366 60.644 1.00 10.52 6 3334 C VAL A 41938.910 67.958 60.419 1.00 12.12 6 3335 O VAL A 419 38.606 69.052 60.8461.00 12.25 8 3336 CB VAL A 419 40.384 66.958 62.145 1.00 11.46 6 3337CG1 VAL A 419 39.231 65.959 62.481 1.00 11.88 6 3338 CG2 VAL A 41941.737 66.266 62.444 1.00 12.56 6 3339 N TYR A 420 38.034 67.172 59.7641.00 11.92 7 3340 CA TYR A 420 36.628 67.548 59.636 1.00 10.72 6 3341 CTYR A 420 35.772 66.328 59.977 1.00 10.50 6 3342 O TYR A 420 35.90865.254 59.383 1.00 13.20 8 3343 CB TYR A 420 36.410 67.866 58.138 1.009.44 6 3344 CG TYR A 420 35.063 68.583 57.856 1.00 10.31 6 3345 CD1 TYRA 420 34.258 69.238 58.754 1.00 13.30 6 3346 CD2 TYR A 420 34.669 68.52356.512 1.00 13.25 6 3347 CE1 TYR A 420 33.045 69.865 58.379 1.00 11.70 63348 CE2 TYR A 420 33.476 69.131 56.115 1.00 14.40 6 3349 CZ TYR A 42032.692 69.780 57.021 1.00 15.49 6 3350 OH TYR A 420 31.503 70.412 56.6831.00 15.26 8 3351 N ILE A 421 35.000 66.508 61.075 1.00 11.61 7 3352 CAILE A 421 34.037 65.462 61.458 1.00 9.13 6 3353 C ILE A 421 32.64966.076 61.282 1.00 10.90 6 3354 O ILE A 421 32.379 67.148 61.788 1.0013.13 8 3355 CB ILE A 421 34.238 64.997 62.941 1.00 11.03 6 3356 CG1 ILEA 421 35.689 64.584 63.133 1.00 11.76 6 3357 CG2 ILE A 421 33.251 63.84163.198 1.00 14.22 6 3358 CD1 ILE A 421 35.980 63.871 64.484 1.00 14.70 63359 N TYR A 422 31.889 65.498 60.276 1.00 10.51 7 3360 CA TYR A 42230.571 66.072 60.004 1.00 11.77 6 3361 C TYR A 422 29.510 64.963 60.0531.00 11.33 6 3362 O TYR A 422 29.877 63.774 59.986 1.00 11.55 8 3363 CBTYR A 422 30.570 66.791 58.623 1.00 11.55 6 3364 CG TYR A 422 31.00065.881 57.458 1.00 12.40 6 3365 CD1 TYR A 422 30.094 65.103 56.724 1.0011.81 6 3366 CD2 TYR A 422 32.354 65.851 57.140 1.00 11.72 6 3367 CE1TYR A 422 30.559 64.305 55.668 1.00 12.09 6 3368 CE2 TYR A 422 32.85365.051 56.094 1.00 11.73 6 3369 CZ TYR A 422 31.935 64.298 55.377 1.0013.04 6 3370 OH TYR A 422 32.365 63.520 54.338 1.00 11.43 8 3371 N GLU A423 28.257 65.380 60.139 1.00 11.98 7 3372 CA GLU A 423 27.202 64.37860.362 1.00 11.04 6 3373 C GLU A 423 26.064 64.598 59.383 1.00 11.74 63374 O GLU A 423 25.644 65.748 59.205 1.00 13.56 8 3375 CB GLU A 42326.633 64.609 61.806 1.00 14.91 6 3376 CG GLU A 423 25.731 63.465 62.2581.00 12.27 6 3377 CD GLU A 423 25.459 63.688 63.796 1.00 13.28 6 3378OE1 GLU A 423 24.947 64.750 64.099 1.00 18.28 8 3379 OE2 GLU A 42325.800 62.682 64.408 1.00 17.49 8 3380 N ARG A 424 25.648 63.541 58.6991.00 12.31 7 3381 CA ARG A 424 24.457 63.621 57.847 1.00 11.64 6 3382 CARG A 424 23.268 63.035 58.643 1.00 13.19 6 3383 O ARG A 424 23.51562.077 59.367 1.00 13.04 8 3384 CB ARG A 424 24.665 62.689 56.620 1.0010.72 6 3385 CG ARG A 424 25.961 63.049 55.805 1.00 10.81 6 3386 CD ARGA 424 25.862 64.465 55.212 1.00 11.09 6 3387 NE ARG A 424 24.666 64.72154.412 1.00 10.91 7 3388 CZ ARG A 424 24.420 64.168 53.207 1.00 11.39 63389 NH1 ARG A 424 25.240 63.308 52.620 1.00 10.62 7 3390 NH2 ARG A 42423.239 64.512 52.596 1.00 10.78 7 3391 N LYS A 425 22.068 63.623 58.5421.00 11.90 7 3392 CA LYS A 425 20.937 63.080 59.290 1.00 11.75 6 3393 CLYS A 425 19.685 63.233 58.443 1.00 15.39 6 3394 O LYS A 425 19.44464.340 58.036 1.00 14.23 8 3395 CB LYS A 425 20.801 63.854 60.626 1.0013.68 6 3396 CG LYS A 425 19.617 63.271 61.494 1.00 14.44 6 3397 CD LYSA 425 19.721 63.992 62.863 1.00 19.53 6 3398 CE LYS A 425 18.739 63.34263.856 1.00 20.97 6 3399 NZ LYS A 425 17.322 63.663 63.509 1.00 23.72 73400 N PHE A 426 18.908 62.144 58.357 1.00 12.33 7 3401 CA PHE A 42617.583 62.238 57.709 1.00 12.03 6 3402 C PHE A 426 16.651 61.481 58.7061.00 11.05 6 3403 O PHE A 426 16.657 60.252 58.693 1.00 13.03 8 3404 CBPHE A 426 17.608 61.450 56.397 1.00 13.23 6 3405 CG PHE A 426 16.26061.449 55.699 1.00 12.58 6 3406 CD1 PHE A 426 15.838 62.659 55.147 1.0014.04 6 3407 CD2 PHE A 426 15.515 60.300 55.571 1.00 14.55 6 3408 CE1PHE A 426 14.594 62.715 54.490 1.00 13.58 6 3409 CE2 PHE A 426 14.26460.345 54.906 1.00 15.67 6 3410 CZ PHE A 426 13.839 61.552 54.398 1.0015.62 6 3411 N PHE A 427 15.916 62.357 59.408 1.00 14.34 7 3412 CA PHE A427 15.024 61.773 60.490 1.00 16.20 6 3413 C PHE A 427 15.781 60.83661.400 1.00 17.32 6 3414 O PHE A 427 16.737 61.354 62.070 1.00 19.10 83415 CB PHE A 427 13.772 61.132 59.840 1.00 18.52 6 3416 CG PHE A 42712.888 62.175 59.193 1.00 17.73 6 3417 CD1 PHE A 427 11.972 62.91859.905 1.00 21.55 6 3418 CD2 PHE A 427 13.018 62.396 57.830 1.00 14.51 63419 CE1 PHE A 427 11.188 63.858 59.276 1.00 18.85 6 3420 CE2 PHE A 42712.246 63.336 57.185 1.00 16.68 6 3421 CZ PHE A 427 11.311 64.087 57.9061.00 19.85 6 3422 N ASN A 428 15.546 59.522 61.442 1.00 15.71 7 3423 CAASN A 428 16.284 58.735 62.433 1.00 17.74 6 3424 C ASN A 428 17.57358.173 61.837 1.00 18.72 6 3425 O ASN A 428 18.307 57.587 62.639 1.0017.57 8 3426 CB ASN A 428 15.484 57.591 63.008 1.00 22.35 6 3427 CG ASNA 428 14.267 58.214 63.733 1.00 36.36 6 3428 OD1 ASN A 428 14.452 59.09264.570 1.00 38.45 8 3429 ND2 ASN A 428 13.103 57.735 63.325 1.00 44.64 73430 N ASP A 429 17.867 58.370 60.547 1.00 15.06 7 3431 CA ASP A 42919.091 57.810 59.986 1.00 14.19 6 3432 C ASP A 429 20.222 58.816 60.1031.00 11.55 6 3433 O ASP A 429 20.026 60.024 59.967 1.00 13.16 8 3434 CBASP A 429 18.927 57.501 58.471 1.00 12.81 6 3435 CG ASP A 429 17.76656.561 58.255 1.00 28.25 6 3436 OD1 ASP A 429 17.727 55.530 58.940 1.0020.84 8 3437 OD2 ASP A 429 16.804 56.870 57.490 1.00 27.47 8 3438 N VALA 430 21.384 58.297 60.600 1.00 12.85 7 3439 CA VAL A 430 22.502 59.19260.876 1.00 11.51 6 3440 C VAL A 430 23.816 58.621 60.371 1.00 13.31 63441 O VAL A 430 23.993 57.405 60.522 1.00 12.49 8 3442 CB VAL A 43022.632 59.315 62.427 1.00 14.21 6 3443 CG1 VAL A 430 23.828 60.23362.734 1.00 14.56 6 3444 CG2 VAL A 430 21.373 59.955 63.033 1.00 14.79 63445 N VAL A 431 24.721 59.432 59.826 1.00 12.54 7 3446 CA VAL A 43126.043 58.933 59.434 1.00 11.58 6 3447 C VAL A 431 27.051 59.978 59.9121.00 11.43 6 3448 O VAL A 431 26.847 61.129 59.603 1.00 12.12 8 3449 CBVAL A 431 26.250 58.685 57.905 1.00 12.54 6 3450 CG1 VAL A 431 27.69858.199 57.615 1.00 10.81 6 3451 CG2 VAL A 431 25.254 57.657 57.400 1.0013.14 6 3452 N LEU A 432 27.976 59.557 60.800 1.00 10.48 7 3453 CA LEU A432 29.015 60.512 61.285 1.00 11.27 6 3454 C LEU A 432 30.317 60.14060.583 1.00 11.12 6 3455 O LEU A 432 30.708 58.961 60.577 1.00 13.28 83456 CB LEU A 432 29.087 60.224 62.831 1.00 11.86 6 3457 CG LEU A 43230.033 61.205 63.562 1.00 11.74 6 3458 CD1 LEU A 432 29.574 62.64363.510 1.00 11.18 6 3459 CD2 LEU A 432 30.119 60.744 65.044 1.00 14.23 63460 N VAL A 433 30.987 61.141 59.978 1.00 11.73 7 3461 CA VAL A 43332.162 60.867 59.131 1.00 9.07 6 3462 C VAL A 433 33.328 61.667 59.7021.00 9.49 6 3463 O VAL A 433 33.158 62.864 59.844 1.00 10.58 8 3464 CBVAL A 433 31.899 61.334 57.674 1.00 10.62 6 3465 CG1 VAL A 433 33.17361.088 56.812 1.00 11.05 6 3466 CG2 VAL A 433 30.693 60.564 57.072 1.0011.15 6 3467 N ALA A 434 34.455 61.000 60.017 1.00 10.65 7 3468 CA ALA A434 35.643 61.757 60.409 1.00 10.07 6 3469 C ALA A 434 36.742 61.60359.363 1.00 11.73 6 3470 O ALA A 434 37.030 60.489 58.924 1.00 11.96 83471 CB ALA A 434 36.199 61.171 61.742 1.00 10.24 6 3472 N ILE A 43537.345 62.744 58.992 1.00 10.23 7 3473 CA ILE A 435 38.438 62.741 58.0081.00 8.82 6 3474 C ILE A 435 39.571 63.587 58.558 1.00 10.58 6 3475 OILE A 435 39.366 64.734 58.922 1.00 10.88 8 3476 CB ILE A 435 37.96163.408 56.674 1.00 10.84 6 3477 CG1 ILE A 435 36.749 62.608 56.120 1.0011.49 6 3478 CG2 ILE A 435 39.146 63.352 55.689 1.00 10.37 6 3479 CD1ILE A 435 36.230 63.228 54.758 1.00 13.59 6 3480 N ASN A 436 40.74162.933 58.596 1.00 10.83 7 3481 CA ASN A 436 41.963 63.646 58.943 1.0011.64 6 3482 C ASN A 436 42.852 63.653 57.715 1.00 9.83 6 3483 O ASN A436 43.367 62.621 57.309 1.00 12.85 8 3484 CB ASN A 436 42.711 62.82160.036 1.00 12.59 6 3485 CG ASN A 436 44.030 63.480 60.383 1.00 12.87 63486 OD1 ASN A 436 44.422 64.602 60.026 1.00 13.07 8 3487 ND2 ASN A 43644.789 62.721 61.224 1.00 13.56 7 3488 N ARG A 437 43.055 64.891 57.1811.00 10.03 7 3489 CA ARG A 437 43.878 64.887 55.958 1.00 9.39 6 3490 CARG A 437 45.362 64.725 56.267 1.00 10.71 6 3491 O ARG A 437 46.11764.552 55.310 1.00 12.32 8 3492 CB ARG A 437 43.673 66.201 55.161 1.0012.80 6 3493 CG ARG A 437 44.296 67.415 55.869 1.00 13.58 6 3494 CD ARGA 437 44.031 68.719 55.043 1.00 11.13 6 3495 NE ARG A 437 44.772 69.84755.738 1.00 10.90 7 3496 CZ ARG A 437 44.957 71.046 55.195 1.00 14.88 63497 NH1 ARG A 437 44.521 71.299 53.948 1.00 11.67 7 3498 NH2 ARG A 43745.406 72.058 55.947 1.00 13.84 7 3499 N ASN A 438 45.779 65.035 57.5131.00 11.11 7 3500 CA ASN A 438 47.255 65.048 57.734 1.00 12.20 6 3501 CASN A 438 47.780 63.623 57.869 1.00 13.73 6 3502 O ASN A 438 47.44062.900 58.830 1.00 12.56 8 3503 CB ASN A 438 47.474 65.787 59.071 1.0013.49 6 3504 CG ASN A 438 48.921 66.167 59.255 1.00 13.92 6 3505 OD1 ASNA 438 49.775 65.335 58.985 1.00 15.45 8 3506 ND2 ASN A 438 49.263 67.37659.700 1.00 13.51 7 3507 N THR A 439 48.650 63.224 56.949 1.00 11.49 73508 CA THR A 439 49.087 61.822 56.883 1.00 12.77 6 3509 C THR A 43950.271 61.585 57.846 1.00 14.69 6 3510 O THR A 439 50.750 60.450 57.9171.00 16.23 8 3511 CB THR A 439 49.518 61.431 55.456 1.00 16.48 6 3512OG1 THR A 439 50.542 62.330 54.990 1.00 17.73 8 3513 CG2 THR A 43948.284 61.611 54.554 1.00 15.47 6 3514 N GLN A 440 50.666 62.669 58.5011.00 14.00 7 3515 CA GLN A 440 51.778 62.467 59.481 1.00 16.61 6 3516 CGLN A 440 51.339 62.729 60.910 1.00 19.80 6 3517 O GLN A 440 52.19862.543 61.812 1.00 18.55 8 3518 CB GLN A 440 52.905 63.422 59.081 1.0023.60 6 3519 CG GLN A 440 53.543 62.971 57.761 1.00 37.17 6 3520 CD GLNA 440 54.248 61.634 57.810 1.00 48.48 6 3521 OE1 GLN A 440 55.292 61.46258.444 1.00 57.64 8 3522 NE2 GLN A 440 53.729 60.605 57.127 1.00 54.59 73523 N SER A 441 50.115 63.161 61.192 1.00 13.09 7 3524 CA SER A 44149.738 63.516 62.559 1.00 13.14 6 3525 C SER A 441 48.481 62.739 62.9581.00 18.60 6 3526 O SER A 441 47.524 62.718 62.168 1.00 15.27 8 3527 CBSER A 441 49.451 65.025 62.702 1.00 16.00 6 3528 OG SER A 441 50.65865.770 62.516 1.00 17.34 8 3529 N SER A 442 48.417 62.251 64.198 1.0013.46 7 3530 CA SER A 442 47.177 61.703 64.730 1.00 13.64 6 3531 C SER A442 46.581 62.835 65.599 1.00 14.33 6 3532 O SER A 442 47.366 63.76165.974 1.00 15.22 8 3533 CB SER A 442 47.452 60.598 65.791 1.00 15.48 63534 OG SER A 442 48.033 59.420 65.203 1.00 19.49 8 3535 N TYR A 44345.302 62.845 65.817 1.00 13.24 7 3536 CA TYR A 443 44.693 63.886 66.6941.00 12.26 6 3537 C TYR A 443 43.877 63.156 67.749 1.00 14.89 6 3538 OTYR A 443 43.032 62.293 67.451 1.00 14.44 8 3539 CB TYR A 443 43.77264.824 65.860 1.00 13.59 6 3540 CG TYR A 443 44.592 65.807 65.009 1.0010.92 6 3541 CD1 TYR A 443 45.124 66.940 65.629 1.00 12.95 6 3542 CD2TYR A 443 44.836 65.549 63.667 1.00 12.89 6 3543 CE1 TYR A 443 45.90867.843 64.882 1.00 11.89 6 3544 CE2 TYR A 443 45.595 66.474 62.914 1.0011.54 6 3545 CZ TYR A 443 46.107 67.595 63.551 1.00 12.16 6 3546 OH TYRA 443 46.871 68.508 62.811 1.00 15.42 8 3547 N SER A 444 43.976 63.66369.008 1.00 14.60 7 3548 CA SER A 444 43.034 63.232 70.040 1.00 14.67 63549 C SER A 444 41.698 64.002 69.912 1.00 13.95 6 3550 O SER A 44441.739 65.229 69.879 1.00 16.35 8 3551 CB SER A 444 43.620 63.684 71.4181.00 17.27 6 3552 OG SER A 444 44.701 62.764 71.733 1.00 18.88 8 3553 NILE A 445 40.628 63.265 69.758 1.00 15.00 7 3554 CA ILE A 445 39.30363.892 69.559 1.00 13.10 6 3555 C ILE A 445 38.498 63.757 70.863 1.0014.11 6 3556 O ILE A 445 37.935 62.703 71.131 1.00 17.51 8 3557 CB ILE A445 38.537 63.188 68.403 1.00 14.59 6 3558 CG1 ILE A 445 39.386 63.12067.136 1.00 15.39 6 3559 CG2 ILE A 445 37.159 63.906 68.223 1.00 16.44 63560 CD1 ILE A 445 39.772 64.500 66.533 1.00 15.53 6 3561 N SER A 44638.309 64.925 71.501 1.00 15.73 7 3562 CA SER A 446 37.450 65.018 72.6801.00 16.64 6 3563 C SER A 446 36.394 66.091 72.415 1.00 18.39 6 3564 OSER A 446 36.592 67.021 71.653 1.00 18.43 8 3565 CB SER A 446 38.24865.398 73.972 1.00 18.77 6 3566 OG SER A 446 38.784 66.689 73.750 1.0024.38 8 3567 N GLY A 447 35.263 65.958 73.091 1.00 19.05 7 3568 CA GLY A447 34.169 66.916 73.050 1.00 17.05 6 3569 C GLY A 447 33.253 66.66071.829 1.00 20.26 6 3570 O GLY A 447 32.491 67.554 71.467 1.00 19.38 83571 N LEU A 448 33.487 65.502 71.171 1.00 13.94 7 3572 CA LEU A 44832.625 65.262 69.967 1.00 15.40 6 3573 C LEU A 448 31.245 64.853 70.3861.00 16.78 6 3574 O LEU A 448 31.018 63.906 71.155 1.00 17.47 8 3575 CBLEU A 448 33.312 64.155 69.144 1.00 14.08 6 3576 CG LEU A 448 32.57863.628 67.903 1.00 15.34 6 3577 CD1 LEU A 448 32.403 64.740 66.845 1.0016.18 6 3578 CD2 LEU A 448 33.283 62.449 67.256 1.00 13.42 6 3579 N GLNA 449 30.221 65.509 69.814 1.00 13.16 7 3580 CA GLN A 449 28.812 65.22470.018 1.00 14.91 6 3581 C GLN A 449 28.209 64.630 68.734 1.00 16.76 63582 O GLN A 449 28.754 64.827 67.645 1.00 13.94 8 3583 CB AGLN A 44928.054 66.486 70.470 0.50 18.23 6 3584 CG AGLN A 449 28.884 67.20671.540 0.50 24.01 6 3585 CD AGLN A 449 28.211 68.188 72.449 0.50 23.44 63586 OE1 AGLN A 449 28.812 68.606 73.455 0.50 32.55 8 3587 NE2 AGLN A449 26.984 68.573 72.134 0.50 32.22 7 3583 CB BGLN A 449 27.974 66.47370.339 0.50 13.26 6 3584 CG BGLN A 449 28.536 67.122 71.620 0.50 17.72 63585 CD BGLN A 449 28.037 66.396 72.844 0.50 16.00 6 3586 OE1 BGLN A 44928.776 65.702 73.511 0.50 22.43 8 3587 NE2 BGLN A 449 26.759 66.55073.145 0.50 23.34 7 3588 N THR A 450 27.085 63.965 68.897 1.00 15.61 73589 CA THR A 450 26.481 63.264 67.761 1.00 13.97 6 3590 C THR A 45024.998 63.001 67.994 1.00 16.43 6 3591 O THR A 450 24.528 62.925 69.1601.00 16.61 8 3592 CB THR A 450 27.216 61.912 67.566 1.00 15.00 6 3593OG1 THR A 450 26.686 61.176 66.471 1.00 15.07 8 3594 CG2 THR A 45027.007 61.016 68.814 1.00 18.27 6 3595 N ALA A 451 24.286 62.806 66.8861.00 15.10 7 3596 CA ALA A 451 22.898 62.330 66.941 1.00 16.96 6 3597 CALA A 451 22.799 60.830 66.879 1.00 15.04 6 3598 O ALA A 451 21.68160.282 66.900 1.00 15.44 8 3599 CB ALA A 451 22.212 62.946 65.681 1.0016.26 6 3600 N LEU A 452 23.929 60.083 66.788 1.00 14.57 7 3601 CA LEU A452 23.803 58.623 66.814 1.00 12.45 6 3602 C LEU A 452 23.170 58.20068.158 1.00 17.32 6 3603 O LEU A 452 23.505 58.727 69.218 1.00 17.00 83604 CB LEU A 452 25.201 57.989 66.779 1.00 14.27 6 3605 CG LEU A 45225.854 58.082 65.380 1.00 14.43 6 3606 CD1 LEU A 452 27.344 57.71665.610 1.00 13.81 6 3607 CD2 LEU A 452 25.263 57.102 64.375 1.00 14.40 63608 N PRO A 453 22.383 57.163 68.080 1.00 16.12 7 3609 CA PRO A 45321.808 56.539 69.305 1.00 18.87 6 3610 C PRO A 453 22.936 55.882 70.0901.00 19.68 6 3611 O PRO A 453 24.039 55.532 69.686 1.00 18.19 8 3612 CBPRO A 453 20.796 55.523 68.880 1.00 20.41 6 3613 CG PRO A 453 20.61555.743 67.392 1.00 21.35 6 3614 CD PRO A 453 21.806 56.582 66.872 1.0016.78 6 3615 N ASN A 454 22.619 55.684 71.406 1.00 14.58 7 3616 CA ASN A454 23.630 55.025 72.244 1.00 14.89 6 3617 C ASN A 454 24.085 53.70471.712 1.00 18.47 6 3618 O ASN A 454 23.320 52.881 71.168 1.00 17.84 83619 CB ASN A 454 22.851 54.705 73.573 1.00 17.80 6 3620 CG ASN A 45422.656 55.933 74.421 1.00 24.08 6 3621 OD1 ASN A 454 23.071 57.05574.201 1.00 19.24 8 3622 ND2 ASN A 454 21.941 55.757 75.554 1.00 24.42 73623 N GLY A 455 25.378 53.451 71.950 1.00 17.75 7 3624 CA GLY A 45525.919 52.156 71.553 1.00 20.13 6 3625 C GLY A 455 27.422 52.289 71.1721.00 17.39 6 3626 O GLY A 455 27.899 53.393 71.080 1.00 19.07 8 3627 NSER A 456 27.916 51.112 70.814 1.00 18.37 7 3628 CA SER A 456 29.28651.073 70.261 1.00 17.34 6 3629 C SER A 456 29.173 50.927 68.725 1.0017.80 6 3630 O SER A 456 28.322 50.199 68.220 1.00 20.53 8 3631 CB SER A456 29.916 49.747 70.778 1.00 22.39 6 3632 OG SER A 456 30.178 49.99872.161 1.00 30.42 8 3633 N TYR A 457 30.024 51.683 68.013 1.00 15.08 73634 CA TYR A 457 29.941 51.627 66.559 1.00 13.18 6 3635 C TYR A 45731.301 51.229 65.961 1.00 14.20 6 3636 O TYR A 457 32.257 51.915 66.2591.00 16.66 8 3637 CB TYR A 457 29.564 53.017 65.941 1.00 17.47 6 3638 CGTYR A 457 28.122 53.387 66.241 1.00 15.26 6 3639 CD1 TYR A 457 27.79953.933 67.497 1.00 15.37 6 3640 CD2 TYR A 457 27.077 53.174 65.325 1.0016.16 6 3641 CE1 TYR A 457 26.521 54.297 67.873 1.00 15.82 6 3642 CE2TYR A 457 25.768 53.516 65.671 1.00 15.99 6 3643 CZ TYR A 457 25.52354.070 66.928 1.00 16.37 6 3644 OH TYR A 457 24.210 54.401 67.218 1.0016.11 8 3645 N ALA A 458 31.329 50.211 65.128 1.00 14.59 7 3646 CA ALA A458 32.601 49.943 64.445 1.00 17.03 6 3647 C ALA A 458 32.686 50.91563.247 1.00 14.66 6 3648 O ALA A 458 31.654 51.326 62.731 1.00 14.84 83649 CB ALA A 458 32.638 48.538 63.857 1.00 17.50 6 3650 N ASP A 45933.942 51.128 62.831 1.00 13.42 7 3651 CA ASP A 459 34.082 51.858 61.5211.00 11.91 6 3652 C ASP A 459 33.472 51.048 60.410 1.00 12.75 6 3653 OASP A 459 33.679 49.834 60.222 1.00 13.42 8 3654 CB ASP A 459 35.56752.007 61.258 1.00 12.66 6 3655 CG ASP A 459 35.984 52.522 59.876 1.0013.56 6 3656 OD1 ASP A 459 35.143 53.232 59.328 1.00 12.36 8 3657 OD2ASP A 459 37.109 52.170 59.441 1.00 14.11 8 3658 N TYR A 460 32.58151.730 59.662 1.00 11.96 7 3659 CA TYR A 460 31.927 51.022 58.513 1.0013.29 6 3660 C TYR A 460 32.905 50.541 57.467 1.00 16.04 6 3661 O TYR A460 32.617 49.627 56.683 1.00 15.32 8 3662 CB TYR A 460 30.909 52.02157.931 1.00 13.60 6 3663 CG TYR A 460 29.970 51.418 56.899 1.00 13.06 63664 CD1 TYR A 460 28.809 50.815 57.400 1.00 11.63 6 3665 CD2 TYR A 46030.215 51.365 55.532 1.00 16.49 6 3666 CE1 TYR A 460 27.838 50.27456.514 1.00 15.86 6 3667 CE2 TYR A 460 29.278 50.783 54.662 1.00 15.66 63668 CZ TYR A 460 28.098 50.257 55.165 1.00 17.45 6 3669 OH TYR A 46027.209 49.696 54.262 1.00 16.44 8 3670 N LEU A 461 34.057 51.242 57.3741.00 13.04 7 3671 CA LEU A 461 35.137 50.814 56.424 1.00 13.89 6 3672 CLEU A 461 36.026 49.742 57.023 1.00 14.71 6 3673 O LEU A 461 36.99249.331 56.369 1.00 13.39 8 3674 CB LEU A 461 35.968 52.115 56.171 1.0013.08 6 3675 CG LEU A 461 35.299 53.075 55.149 1.00 13.44 6 3676 CD1 LEUA 461 35.968 54.453 55.284 1.00 14.44 6 3677 CD2 LEU A 461 35.485 52.52653.743 1.00 16.37 6 3678 N SER A 462 35.746 49.218 58.222 1.00 15.11 73679 CA SER A 462 36.521 48.122 58.810 1.00 16.17 6 3680 C SER A 46238.011 48.422 58.907 1.00 17.10 6 3681 O SER A 462 38.878 47.546 58.7631.00 16.40 8 3682 CB SER A 462 36.316 46.813 57.987 1.00 19.17 6 3683 OGSER A 462 34.914 46.479 57.974 1.00 20.76 8 3684 N GLY A 463 38.36949.689 59.115 1.00 13.98 7 3685 CA GLY A 463 39.781 50.089 59.271 1.0014.97 6 3686 C GLY A 463 40.533 50.140 57.949 1.00 15.42 6 3687 O GLY A463 41.745 50.387 57.984 1.00 15.84 8 3688 N LEU A 464 39.816 50.04356.808 1.00 12.86 7 3689 CA LEU A 464 40.559 50.113 55.525 1.00 10.93 63690 C LEU A 464 41.370 51.420 55.427 1.00 12.62 6 3691 O LEU A 46442.484 51.408 54.854 1.00 14.36 8 3692 CB LEU A 464 39.487 50.148 54.4021.00 13.24 6 3693 CG LEU A 464 40.083 50.223 52.969 1.00 14.42 6 3694CD1 LEU A 464 40.800 48.892 52.620 1.00 15.93 6 3695 CD2 LEU A 46438.971 50.469 51.967 1.00 14.00 6 3696 N LEU A 465 40.797 52.526 55.8721.00 11.79 7 3697 CA LEU A 465 41.473 53.824 55.761 1.00 12.51 6 3698 CLEU A 465 41.953 54.319 57.114 1.00 13.32 6 3699 O LEU A 465 41.87355.518 57.401 1.00 16.12 8 3700 CB LEU A 465 40.510 54.894 55.130 1.0012.90 6 3701 CG LEU A 465 40.090 54.441 53.714 1.00 12.88 6 3702 CD1 LEUA 465 39.162 55.509 53.111 1.00 14.96 6 3703 CD2 LEU A 465 41.263 54.19152.777 1.00 14.83 6 3704 N GLY A 466 42.237 53.348 58.043 1.00 14.06 73705 CA GLY A 466 42.789 53.800 59.336 1.00 14.74 6 3706 C GLY A 46641.735 54.095 60.400 1.00 14.06 6 3707 O GLY A 466 42.061 54.643 61.4791.00 15.13 8 3708 N GLY A 467 40.451 53.817 60.125 1.00 13.86 7 3709 CAGLY A 467 39.357 54.137 61.045 1.00 11.80 6 3710 C GLY A 467 39.32153.244 62.311 1.00 14.35 6 3711 O GLY A 467 40.083 52.261 62.394 1.0016.59 8 3712 N ASN A 468 38.509 53.696 63.236 1.00 15.29 7 3713 CA ASN A468 38.483 53.050 64.569 1.00 14.61 6 3714 C ASN A 468 37.007 52.96064.963 1.00 15.14 6 3715 O ASN A 468 36.145 53.679 64.418 1.00 15.07 83716 CB ASN A 468 39.253 54.012 65.515 1.00 16.45 6 3717 CG ASN A 46838.730 55.429 65.538 1.00 17.15 6 3718 OD1 ASN A 468 39.013 56.37564.739 1.00 19.92 8 3719 ND2 ASN A 468 37.812 55.710 66.490 1.00 16.39 73720 N GLY A 469 36.787 52.285 66.076 1.00 16.49 7 3721 CA GLY A 46935.415 52.189 66.624 1.00 16.85 6 3722 C GLY A 469 35.261 53.309 67.6401.00 14.55 6 3723 O GLY A 469 36.191 53.919 68.176 1.00 17.51 8 3724 NILE A 470 33.976 53.624 67.954 1.00 14.83 7 3725 CA ILE A 470 33.62354.650 68.921 1.00 14.09 6 3726 C ILE A 470 32.518 54.102 69.860 1.0013.92 6 3727 O ILE A 470 31.867 53.108 69.553 1.00 19.57 8 3728 CB ILE A470 33.155 56.004 68.368 1.00 16.37 6 3729 CG1 ILE A 470 31.948 55.75367.429 1.00 17.51 6 3730 CG2 ILE A 470 34.319 56.652 67.581 1.00 16.76 63731 CD1 ILE A 470 31.315 57.104 67.032 1.00 15.78 6 3732 N SER A 47132.408 54.804 70.980 1.00 15.71 7 3733 CA SER A 471 31.268 54.477 71.9031.00 14.51 6 3734 C SER A 471 30.497 55.755 72.165 1.00 14.83 6 3735 OSER A 471 31.107 56.814 72.402 1.00 17.55 8 3736 CB SER A 471 32.02454.018 73.220 1.00 22.00 6 3737 OG SER A 471 30.967 53.933 74.176 1.0027.40 8 3738 N VAL A 472 29.172 55.712 72.054 1.00 14.69 7 3739 CA VAL A472 28.298 56.834 72.186 1.00 14.15 6 3740 C VAL A 472 27.380 56.69673.425 1.00 15.07 6 3741 O VAL A 472 26.764 55.638 73.563 1.00 19.05 83742 CB VAL A 472 27.433 56.903 70.900 1.00 15.53 6 3743 CG1 VAL A 47226.446 58.057 70.970 1.00 14.81 6 3744 CG2 VAL A 472 28.376 57.15369.691 1.00 18.40 6 3745 N SER A 473 27.351 57.767 74.184 1.00 15.80 73746 CA SER A 473 26.386 57.736 75.312 1.00 16.44 6 3747 C SER A 47325.711 59.073 75.420 1.00 16.40 6 3748 O SER A 473 26.435 60.084 75.5481.00 19.98 8 3749 CB SER A 473 27.214 57.446 76.594 1.00 21.00 6 3750 OGSER A 473 26.284 57.573 77.686 1.00 31.70 8 3751 N ASN A 474 24.39659.107 75.308 1.00 18.40 7 3752 CA ASN A 474 23.632 60.348 75.444 1.0019.45 6 3753 C ASN A 474 24.194 61.523 74.646 1.00 19.99 6 3754 O ASN A474 24.363 62.658 75.103 1.00 15.86 8 3755 CB ASN A 474 23.685 60.70776.968 1.00 22.35 6 3756 CG ASN A 474 22.991 59.572 77.722 1.00 31.24 63757 OD1 ASN A 474 22.086 58.887 77.191 1.00 33.57 8 3758 ND2 ASN A 47423.579 59.303 78.890 1.00 32.67 7 3759 N GLY A 475 24.452 61.223 73.3411.00 17.78 7 3760 CA GLY A 475 24.866 62.311 72.438 1.00 20.56 6 3761 CGLY A 475 26.369 62.573 72.430 1.00 18.34 6 3762 O GLY A 475 26.80763.464 71.690 1.00 20.59 8 3763 N SER A 476 27.146 61.894 73.305 1.0018.39 7 3764 CA SER A 476 28.563 62.222 73.451 1.00 14.26 6 3765 C SER A476 29.384 61.026 72.974 1.00 17.38 6 3766 O SER A 476 29.103 59.90273.358 1.00 18.38 8 3767 CB ASER A 476 28.931 62.557 74.900 0.70 19.66 63768 OG ASER A 476 28.330 63.803 75.257 0.70 22.12 8 3767 CB BSER A 47628.870 62.465 74.932 0.30 18.16 6 3768 OG BSER A 476 30.220 62.82275.127 0.30 20.85 8 3769 N VAL A 477 30.430 61.284 72.188 1.00 15.08 73770 CA VAL A 477 31.322 60.248 71.766 1.00 16.01 6 3771 C VAL A 47732.549 60.211 72.699 1.00 14.42 6 3772 O VAL A 477 33.117 61.277 72.9131.00 16.73 8 3773 CB VAL A 477 31.852 60.539 70.320 1.00 12.17 6 3774CG1 VAL A 477 32.718 59.377 69.872 1.00 15.08 6 3775 CG2 VAL A 47730.665 60.682 69.389 1.00 13.12 6 3776 N ALA A 478 32.802 59.035 73.2361.00 17.39 7 3777 CA ALA A 478 33.956 58.962 74.181 1.00 17.45 6 3778 CALA A 478 35.248 59.401 73.501 1.00 19.79 6 3779 O ALA A 478 35.39859.204 72.298 1.00 15.95 8 3780 CB ALA A 478 34.031 57.543 74.731 1.0018.76 6 3781 N SER A 479 36.152 60.069 74.181 1.00 15.72 7 3782 CA SER A479 37.405 60.518 73.501 1.00 17.20 6 3783 C SER A 479 38.170 59.39272.855 1.00 16.18 6 3784 O SER A 479 38.177 58.231 73.329 1.00 16.38 83785 CB SER A 479 38.262 61.218 74.569 1.00 23.12 6 3786 OG SER A 47937.554 62.348 75.047 1.00 22.40 8 3787 N PHE A 480 38.774 59.656 71.6741.00 16.00 7 3788 CA PHE A 480 39.449 58.638 70.881 1.00 15.01 6 3789 CPHE A 480 40.575 59.308 70.092 1.00 14.53 6 3790 O PHE A 480 40.56860.548 70.019 1.00 17.08 8 3791 CB PHE A 480 38.538 57.834 69.938 1.0014.92 6 3792 CG PHE A 480 37.888 58.695 68.846 1.00 15.98 6 3793 CD1 PHEA 480 36.748 59.437 69.087 1.00 14.48 6 3794 CD2 PHE A 480 38.493 58.72867.589 1.00 14.19 6 3795 CE1 PHE A 480 36.160 60.227 68.092 1.00 18.16 63796 CE2 PHE A 480 37.899 59.513 66.609 1.00 18.21 6 3797 CZ PHE A 48036.770 60.255 66.848 1.00 19.62 6 3798 N THR A 481 41.459 58.476 69.5651.00 15.04 7 3799 CA THR A 481 42.525 59.036 68.696 1.00 12.66 6 3800 CTHR A 481 42.186 58.783 67.223 1.00 14.82 6 3801 O THR A 481 41.81157.641 66.885 1.00 16.40 8 3802 CB THR A 481 43.859 58.332 69.002 1.0019.94 6 3803 OG1 THR A 481 44.253 58.543 70.360 1.00 21.84 8 3804 CG2THR A 481 44.953 58.894 68.091 1.00 20.55 6 3805 N LEU A 482 42.21659.860 66.454 1.00 14.98 7 3806 CA LEU A 482 42.004 59.690 64.991 1.0013.06 6 3807 C LEU A 482 43.383 59.527 64.394 1.00 14.32 6 3808 O LEU A482 44.199 60.432 64.487 1.00 15.20 8 3809 CB LEU A 482 41.231 60.91764.486 1.00 13.14 6 3810 CG LEU A 482 40.812 60.936 62.999 1.00 14.96 63811 CD1 LEU A 482 39.938 59.717 62.720 1.00 16.24 6 3812 CD2 LEU A 48240.073 62.242 62.727 1.00 14.36 6 3813 N ALA A 483 43.621 58.414 63.6801.00 12.65 7 3814 CA ALA A 483 44.961 58.090 63.175 1.00 13.54 6 3815 CALA A 483 45.370 58.961 62.000 1.00 13.15 6 3816 O ALA A 483 44.56259.723 61.387 1.00 13.10 8 3817 CB ALA A 483 44.892 56.581 62.782 1.0012.82 6 3818 N PRO A 484 46.637 58.980 61.687 1.00 14.66 7 3819 CA PRO A484 47.183 59.827 60.632 1.00 11.27 6 3820 C PRO A 484 46.509 59.49659.301 1.00 12.98 6 3821 O PRO A 484 46.374 58.331 58.884 1.00 13.40 83822 CB PRO A 484 48.704 59.546 60.545 1.00 15.48 6 3823 CG PRO A 48448.959 58.945 61.936 1.00 15.92 6 3824 CD PRO A 484 47.698 58.160 62.3331.00 15.61 6 3825 N GLY A 485 45.977 60.548 58.671 1.00 14.03 7 3826 CAGLY A 485 45.399 60.352 57.309 1.00 13.19 6 3827 C GLY A 485 44.06759.600 57.376 1.00 16.21 6 3828 O GLY A 485 43.561 59.235 56.271 1.0013.21 8 3829 N ALA A 486 43.508 59.349 58.553 1.00 11.65 7 3830 CA ALA A486 42.375 58.395 58.545 1.00 13.98 6 3831 C ALA A 486 41.058 58.96958.068 1.00 15.41 6 3832 O ALA A 486 40.730 60.148 58.196 1.00 13.33 83833 CB ALA A 486 42.233 57.937 60.002 1.00 14.43 6 3834 N VAL A 48740.213 58.008 57.647 1.00 12.17 7 3835 CA VAL A 487 38.776 58.220 57.4031.00 9.79 6 3836 C VAL A 487 38.057 57.174 58.257 1.00 9.96 6 3837 O VALA 487 38.406 55.970 58.179 1.00 12.30 8 3838 CB VAL A 487 38.428 58.02255.919 1.00 10.95 6 3839 CG1 VAL A 487 36.871 58.150 55.762 1.00 12.89 63840 CG2 VAL A 487 39.127 58.990 54.964 1.00 15.13 6 3841 N SER A 48837.112 57.635 59.078 1.00 11.84 7 3842 CA SER A 488 36.335 56.623 59.8651.00 12.18 6 3843 C SER A 488 34.867 56.972 59.699 1.00 11.64 6 3844 OSER A 488 34.519 58.154 59.650 1.00 12.81 8 3845 CB SER A 488 36.85056.705 61.336 1.00 15.82 6 3846 OG SER A 488 36.431 55.439 61.907 1.0019.75 8 3847 N VAL A 489 33.950 55.975 59.626 1.00 11.85 7 3848 CA VAL A489 32.567 56.313 59.340 1.00 11.74 6 3849 C VAL A 489 31.685 55.45760.269 1.00 12.51 6 3850 O VAL A 489 31.910 54.276 60.410 1.00 13.59 83851 CB VAL A 489 32.231 55.903 57.882 1.00 12.50 6 3852 CG1 VAL A 48930.712 56.154 57.650 1.00 11.14 6 3853 CG2 VAL A 489 32.978 56.81256.882 1.00 13.14 6 3854 N TRP A 490 30.771 56.135 60.914 1.00 11.35 73855 CA TRP A 490 29.900 55.413 61.883 1.00 11.90 6 3856 C TRP A 49028.446 55.715 61.508 1.00 13.16 6 3857 O TRP A 490 28.103 56.878 61.3241.00 16.40 8 3858 CB TRP A 490 30.222 55.953 63.283 1.00 12.61 6 3859 CGTRP A 490 31.708 55.807 63.639 1.00 12.91 6 3860 CD1 TRP A 490 32.38154.628 63.904 1.00 14.71 6 3861 CD2 TRP A 490 32.632 56.884 63.716 1.0014.18 6 3862 NE1 TRP A 490 33.717 54.969 64.166 1.00 13.76 7 3863 CE2TRP A 490 33.883 56.328 64.049 1.00 14.41 6 3864 CE3 TRP A 490 32.50958.271 63.546 1.00 16.82 6 3865 CZ2 TRP A 490 35.020 57.117 64.216 1.0013.91 6 3866 CZ3 TRP A 490 33.641 59.052 63.701 1.00 14.61 6 3867 CH2TRP A 490 34.894 58.461 64.044 1.00 14.54 6 3868 N GLN A 491 27.68054.618 61.394 1.00 11.75 7 3869 CA GLN A 491 26.332 54.869 60.903 1.0012.20 6 3870 C GLN A 491 25.221 54.121 61.637 1.00 13.63 6 3871 O GLN A491 25.472 53.092 62.207 1.00 13.45 8 3872 CB GLN A 491 26.259 54.45259.410 1.00 12.17 6 3873 CG GLN A 491 26.541 52.972 59.117 1.00 12.78 63874 CD GLN A 491 25.208 52.219 58.993 1.00 19.79 6 3875 OE1 GLN A 49124.222 52.726 58.485 1.00 16.61 8 3876 NE2 GLN A 491 25.214 50.95259.455 1.00 19.28 7 3877 N TYR A 492 24.024 54.698 61.523 1.00 13.67 73878 CA TYR A 492 22.819 54.043 62.092 1.00 14.21 6 3879 C TYR A 49221.665 54.203 61.102 1.00 17.30 6 3880 O TYR A 492 21.507 55.341 60.6141.00 14.76 8 3881 CB TYR A 492 22.452 54.774 63.393 1.00 15.27 6 3882 CGTYR A 492 21.152 54.219 63.984 1.00 15.56 6 3883 CD1 TYR A 492 21.14653.010 64.638 1.00 20.95 6 3884 CD2 TYR A 492 19.963 54.959 63.800 1.0018.48 6 3885 CE1 TYR A 492 19.956 52.511 65.176 1.00 21.55 6 3886 CE2TYR A 492 18.770 54.444 64.324 1.00 19.51 6 3887 CZ TYR A 492 18.81753.254 65.003 1.00 22.52 6 3888 OH TYR A 492 17.596 52.781 65.511 1.0024.89 8 3889 N SER A 493 20.879 53.151 60.925 1.00 15.17 7 3890 CA SER A493 19.666 53.363 60.096 1.00 14.91 6 3891 C SER A 493 18.548 52.46260.616 1.00 20.17 6 3892 O SER A 493 18.887 51.457 61.265 1.00 22.90 83893 CB SER A 493 19.867 53.083 58.619 1.00 23.97 6 3894 OG SER A 49320.148 51.710 58.532 1.00 30.62 8 3895 N THR A 494 17.344 52.991 60.3931.00 15.89 7 3896 CA THR A 494 16.243 52.127 60.906 1.00 18.40 6 3897 CTHR A 494 14.999 52.406 60.060 1.00 20.14 6 3898 O THR A 494 14.96753.429 59.367 1.00 20.45 8 3899 CB THR A 494 15.993 52.424 62.396 1.0024.38 6 3900 OG1 THR A 494 15.137 51.363 62.864 1.00 25.66 8 3901 CG2THR A 494 15.368 53.751 62.737 1.00 27.09 6 3902 N SER A 495 14.01751.534 60.157 1.00 22.56 7 3903 CA SER A 495 12.772 51.870 59.422 1.0019.72 6 3904 C SER A 495 12.082 53.049 60.021 1.00 19.50 6 3905 O SER A495 12.132 53.418 61.188 1.00 21.11 8 3906 CB ASER A 495 11.766 50.69859.444 0.60 26.59 6 3907 OG ASER A 495 12.447 49.487 59.259 0.60 31.40 83907 CB BSER A 495 11.888 50.603 59.441 0.40 20.10 6 3908 OG BSER A 49511.922 50.184 60.798 0.40 20.04 8 3908 N ALA A 496 11.315 53.727 59.1411.00 20.53 7 3909 CA ALA A 496 10.529 54.893 59.493 1.00 21.55 6 3910 CALA A 496 9.094 54.492 59.960 1.00 24.11 6 3911 O ALA A 496 8.536 53.59659.350 1.00 29.93 8 3912 CB ALA A 496 10.354 55.717 58.189 1.00 22.92 63913 N SER A 497 8.599 55.279 60.902 1.00 26.84 7 3914 CA SER A 4977.226 54.967 61.354 1.00 32.64 6 3915 C SER A 497 6.242 56.009 60.8531.00 31.20 6 3916 O SER A 497 5.049 55.788 61.090 1.00 33.40 8 3917 CBSER A 497 7.183 54.836 62.875 1.00 35.13 6 3918 OG SER A 497 7.57856.030 63.515 1.00 39.06 8 3919 N ALA A 498 6.685 56.920 59.967 1.0025.21 7 3920 CA ALA A 498 5.749 57.878 59.354 1.00 21.05 6 3921 C ALA A498 6.350 58.189 57.975 1.00 22.00 6 3922 O ALA A 498 7.541 57.90757.763 1.00 18.25 8 3923 CB ALA A 498 5.737 59.103 60.231 1.00 22.15 63924 N PRO A 499 5.633 58.771 57.054 1.00 18.84 7 3925 CA PRO A 4996.176 59.058 55.718 1.00 19.31 6 3926 C PRO A 499 7.174 60.210 55.7621.00 15.69 6 3927 O PRO A 499 6.934 61.242 56.370 1.00 16.96 8 3928 CBPRO A 499 4.930 59.294 54.823 1.00 20.07 6 3929 CG PRO A 499 3.92759.790 55.829 1.00 23.72 6 3930 CD PRO A 499 4.205 59.113 57.173 1.0023.70 6 3931 N GLN A 500 8.288 59.975 55.037 1.00 18.24 7 3932 CA GLN A500 9.423 60.939 55.075 1.00 13.65 6 3933 C GLN A 500 9.921 61.08453.596 1.00 12.93 6 3934 O GLN A 500 10.256 60.065 53.014 1.00 15.78 83935 CB GLN A 500 10.601 60.286 55.860 1.00 15.18 6 3936 CG GLN A 50010.189 60.048 57.328 1.00 16.32 6 3937 CD GLN A 500 11.284 59.264 58.1261.00 15.95 6 3938 OE1 GLN A 500 12.239 58.781 57.571 1.00 17.99 8 3939NE2 GLN A 500 11.008 59.238 59.419 1.00 20.52 7 3940 N ILE A 501 9.66262.283 53.054 1.00 12.81 7 3941 CA ILE A 501 10.101 62.501 51.667 1.0012.56 6 3942 C ILE A 501 11.594 62.914 51.642 1.00 13.47 6 3943 O ILE A501 11.899 63.905 52.301 1.00 14.35 8 3944 CB ILE A 501 9.262 63.63551.032 1.00 12.51 6 3945 CG1 ILE A 501 7.788 63.216 50.842 1.00 14.81 63946 CG2 ILE A 501 9.888 63.939 49.629 1.00 12.71 6 3947 CD1 ILE A 5016.897 64.308 50.244 1.00 15.70 6 3948 N GLY A 502 12.383 62.169 50.8721.00 12.33 7 3949 CA GLY A 502 13.793 62.673 50.746 1.00 12.41 6 3950 CGLY A 502 13.915 63.416 49.403 1.00 11.68 6 3951 O GLY A 502 14.80664.300 49.332 1.00 12.18 8 3952 N SER A 503 13.120 63.068 48.395 1.0012.99 7 3953 CA SER A 503 13.334 63.710 47.073 1.00 12.73 6 3954 C SER A503 11.970 63.672 46.342 1.00 14.01 6 3955 O SER A 503 11.263 62.67846.449 1.00 14.22 8 3956 CB SER A 503 14.364 62.853 46.296 1.00 12.66 63957 OG SER A 503 14.467 63.267 44.940 1.00 12.94 8 3958 N VAL A 50411.736 64.763 45.625 1.00 12.13 7 3959 CA VAL A 504 10.738 64.716 44.5211.00 11.27 6 3960 C VAL A 504 11.521 65.159 43.243 1.00 11.68 6 3961 OVAL A 504 12.287 66.121 43.321 1.00 11.43 8 3962 CB VAL A 504 9.61465.700 44.790 1.00 12.52 6 3963 CG1 VAL A 504 8.670 65.766 43.563 1.0015.49 6 3964 CG2 VAL A 504 8.740 65.263 46.021 1.00 12.38 6 3965 N ALA A505 11.424 64.285 42.236 1.00 11.00 7 3966 CA ALA A 505 12.174 64.59541.003 1.00 10.56 6 3967 C ALA A 505 11.447 64.174 39.798 1.00 12.28 63968 O ALA A 505 10.738 63.165 39.919 1.00 13.54 8 3969 CB ALA A 50513.567 63.894 41.072 1.00 11.90 6 3970 N PRO A 506 11.674 64.766 38.6611.00 12.95 7 3971 CA PRO A 506 12.353 66.020 38.410 1.00 11.12 6 3972 CPRO A 506 11.747 67.182 39.194 1.00 12.55 6 3973 O PRO A 506 10.71167.015 39.862 1.00 12.33 8 3974 CB PRO A 506 12.227 66.313 36.887 1.0013.30 6 3975 CG PRO A 506 11.545 65.090 36.310 1.00 15.76 6 3976 CD PROA 506 11.007 64.329 37.471 1.00 14.19 6 3977 N ASN A 507 12.364 68.38139.142 1.00 10.92 7 3978 CA ASN A 507 11.835 69.493 39.909 1.00 11.12 63979 C ASN A 507 10.940 70.447 39.087 1.00 10.54 6 3980 O ASN A 50710.497 71.416 39.701 1.00 12.30 8 3981 CB ASN A 507 13.043 70.353 40.4011.00 11.79 6 3982 CG ASN A 507 14.033 69.459 41.196 1.00 14.07 6 3983OD1 ASN A 507 15.192 69.361 40.778 1.00 13.37 8 3984 ND2 ASN A 50713.592 68.845 42.261 1.00 13.47 7 3985 N MET A 508 10.654 70.046 37.8501.00 10.20 7 3986 CA MET A 508 9.823 70.957 37.021 1.00 11.04 6 3987 CMET A 508 9.102 70.087 36.027 1.00 11.63 6 3988 O MET A 508 9.633 69.02935.633 1.00 12.66 8 3989 CB MET A 508 10.929 71.782 36.219 1.00 12.80 63990 CG MET A 508 10.270 72.808 35.305 1.00 15.57 6 3991 SD MET A 50811.558 73.692 34.325 1.00 12.60 16 3992 CE MET A 508 11.921 72.58233.003 1.00 11.82 6 3993 N GLY A 509 7.935 70.545 35.550 1.00 11.36 73994 CA GLY A 509 7.253 69.739 34.528 1.00 10.02 6 3995 C GLY A 5095.851 70.331 34.276 1.00 13.18 6 3996 O GLY A 509 5.506 71.321 34.8891.00 13.82 8 3997 N ILE A 510 5.070 69.599 33.480 1.00 11.23 7 3998 CAILE A 510 3.674 70.061 33.192 1.00 12.19 6 3999 C ILE A 510 2.746 68.96433.701 1.00 11.61 6 4000 O ILE A 510 3.156 67.806 33.903 1.00 13.58 84001 CB ILE A 510 3.456 70.272 31.683 1.00 12.75 6 4002 CG1 ILE A 5103.840 69.011 30.868 1.00 11.82 6 4003 CG2 ILE A 510 4.241 71.485 31.1631.00 14.82 6 4004 CD1 ILE A 510 3.293 69.108 29.417 1.00 18.53 6 4005 NPRO A 511 1.462 69.267 33.824 1.00 13.51 7 4006 CA PRO A 511 0.44268.291 34.164 1.00 14.15 6 4007 C PRO A 511 0.531 67.082 33.263 1.0013.29 6 4008 O PRO A 511 0.780 67.180 32.026 1.00 13.86 8 4009 CB PRO A511 −0.913 69.037 33.810 1.00 13.10 6 4010 CG PRO A 511 −0.528 70.43534.265 1.00 15.94 6 4011 CD PRO A 511 0.925 70.625 33.729 1.00 16.03 64012 N GLY A 512 0.462 65.892 33.876 1.00 12.55 7 4013 CA GLY A 5120.554 64.629 33.165 1.00 14.21 6 4014 C GLY A 512 1.950 63.971 33.1701.00 13.76 6 4015 O GLY A 512 2.002 62.765 32.923 1.00 15.31 8 4016 NASN A 513 2.994 64.789 33.454 1.00 12.18 7 4017 CA ASN A 513 4.30664.154 33.561 1.00 10.79 6 4018 C ASN A 513 4.360 63.144 34.731 1.0015.27 6 4019 O ASN A 513 3.699 63.392 35.738 1.00 13.64 8 4020 CB ASN A513 5.408 65.230 33.833 1.00 11.43 6 4021 CG ASN A 513 5.762 66.02332.583 1.00 11.94 6 4022 OD1 ASN A 513 6.738 66.874 32.746 1.00 16.21 84023 ND2 ASN A 513 5.078 65.931 31.505 1.00 8.90 7 4024 N VAL A 5145.280 62.177 34.576 1.00 11.74 7 4025 CA VAL A 514 5.505 61.269 35.7451.00 11.63 6 4026 C VAL A 514 6.594 61.894 36.612 1.00 13.73 6 4027 OVAL A 514 7.617 62.379 36.131 1.00 15.35 8 4028 CB VAL A 514 6.07259.931 35.221 1.00 13.67 6 4029 CG1 VAL A 514 6.529 59.036 36.390 1.0014.35 6 4030 CG2 VAL A 514 5.042 59.176 34.393 1.00 16.73 6 4031 N VAL A515 6.335 61.959 37.923 1.00 10.41 7 4032 CA VAL A 515 7.256 62.49638.927 1.00 12.67 6 4033 C VAL A 515 7.433 61.442 40.001 1.00 13.31 64034 O VAL A 515 6.495 60.711 40.306 1.00 14.78 8 4035 CB VAL A 5156.563 63.772 39.511 1.00 14.30 6 4036 CG1 VAL A 515 7.228 64.271 40.7751.00 18.11 6 4037 CG2 VAL A 515 6.678 64.883 38.435 1.00 16.90 6 4038 NTHR A 516 8.669 61.321 40.514 1.00 11.19 7 4039 CA THR A 516 8.90060.252 41.495 1.00 11.78 6 4040 C THR A 516 9.271 60.860 42.835 1.0011.71 6 4041 O THR A 516 10.092 61.763 42.959 1.00 12.89 8 4042 CB THR A516 10.107 59.384 41.001 1.00 14.88 6 4043 OG1 THR A 516 9.696 58.78939.742 1.00 14.59 8 4044 CG2 THR A 516 10.446 58.275 42.004 1.00 14.18 64045 N ILE A 517 8.600 60.281 43.863 1.00 9.66 7 4046 CA ILE A 517 8.87860.681 45.251 1.00 10.17 6 4047 C ILE A 517 9.670 59.586 45.920 1.0013.57 6 4048 O ILE A 517 9.172 58.427 45.949 1.00 13.82 8 4049 CB ILE A517 7.493 60.899 45.948 1.00 12.16 6 4050 CG1 ILE A 517 6.659 61.98445.278 1.00 15.38 6 4051 CG2 ILE A 517 7.745 61.419 47.392 1.00 14.69 64052 CD1 ILE A 517 5.200 61.951 45.779 1.00 22.16 6 4053 N ASP A 51810.911 59.861 46.363 1.00 13.29 7 4054 CA ASP A 518 11.743 58.802 46.9761.00 14.12 6 4055 C ASP A 518 11.868 59.161 48.435 1.00 13.11 6 4056 OASP A 518 11.922 60.347 48.791 1.00 14.37 8 4057 CB ASP A 518 13.15958.791 46.351 1.00 14.49 6 4058 CG ASP A 518 13.106 58.207 44.962 1.0017.62 6 4059 OD1 ASP A 518 12.858 56.963 44.888 1.00 17.47 8 4060 OD2ASP A 518 13.289 58.874 43.931 1.00 16.96 8 4061 N GLY A 519 11.76958.138 49.315 1.00 13.39 7 4062 CA GLY A 519 11.872 58.484 50.757 1.0014.21 6 4063 C GLY A 519 11.716 57.152 51.549 1.00 13.61 6 4064 O GLY A519 12.278 56.130 51.134 1.00 15.70 8 4065 N LYS A 520 11.059 57.31952.696 1.00 17.22 7 4066 CA LYS A 520 10.867 56.091 53.545 1.00 15.85 64067 C LYS A 520 9.539 56.230 54.256 1.00 16.54 6 4068 O LYS A 520 9.00457.334 54.385 1.00 17.43 8 4069 CB LYS A 520 11.866 56.344 54.747 1.0017.75 6 4070 CG LYS A 520 13.318 56.307 54.421 1.00 24.98 6 4071 CD LYSA 520 14.147 56.512 55.698 1.00 22.21 6 4072 CE LYS A 520 14.074 55.14556.459 1.00 23.54 6 4073 NZ LYS A 520 15.426 54.879 57.005 1.00 27.08 74074 N GLY A 521 9.021 55.065 54.728 1.00 16.42 7 4075 CA GLY A 5217.870 55.223 55.627 1.00 16.98 6 4076 C GLY A 521 6.540 55.347 54.8741.00 19.49 6 4077 O GLY A 521 5.533 55.716 55.525 1.00 18.22 8 4078 NPHE A 522 6.569 55.053 53.560 1.00 19.15 7 4079 CA PHE A 522 5.29955.230 52.839 1.00 17.53 6 4080 C PHE A 522 4.344 54.037 53.029 1.0020.57 6 4081 O PHE A 522 3.173 54.222 52.638 1.00 20.45 8 4082 CB PHE A522 5.587 55.448 51.342 1.00 17.55 6 4083 CG PHE A 522 6.513 56.60551.009 1.00 15.40 6 4084 CD1 PHE A 522 6.601 57.740 51.763 1.00 17.48 64085 CD2 PHE A 522 7.262 56.452 49.824 1.00 17.80 6 4086 CE1 PHE A 5227.480 58.778 51.376 1.00 20.21 6 4087 CE2 PHE A 522 8.142 57.475 49.4221.00 16.35 6 4088 CZ PHE A 522 8.257 58.607 50.214 1.00 14.66 6 4089 NGLY A 523 4.826 52.902 53.488 1.00 23.38 7 4090 CA GLY A 523 3.94751.721 53.586 1.00 26.21 6 4091 C GLY A 523 3.753 51.037 52.260 1.0027.39 6 4092 O GLY A 523 4.082 51.536 51.167 1.00 21.64 8 4093 N THR A524 3.204 49.785 52.316 1.00 26.00 7 4094 CA THR A 524 3.043 49.01051.103 1.00 24.30 6 4095 C THR A 524 1.636 49.241 50.556 1.00 26.74 64096 O THR A 524 1.433 48.984 49.372 1.00 34.03 8 4097 CB THR A 5243.314 47.505 51.308 1.00 36.63 6 4098 OG1 THR A 524 2.403 47.020 52.3151.00 34.71 8 4099 CG2 THR A 524 4.711 47.251 51.862 1.00 34.40 6 4100 NTHR A 525 0.748 49.673 51.432 1.00 27.38 7 4101 CA THR A 525 −0.64649.948 51.027 1.00 29.73 6 4102 C THR A 525 −0.696 51.367 50.456 1.0029.44 6 4103 O THR A 525 −0.315 52.313 51.159 1.00 28.46 8 4104 CB THR A525 −1.558 49.835 52.265 1.00 31.59 6 4105 OG1 THR A 525 −1.416 48.48552.779 1.00 34.50 8 4106 CG2 THR A 525 −3.020 50.076 51.920 1.00 33.53 64107 N GLN A 526 −1.341 51.530 49.304 1.00 26.38 7 4108 CA GLN A 526−1.383 52.864 48.695 1.00 27.25 6 4109 C GLN A 526 −2.090 53.867 49.5741.00 29.32 6 4110 O GLN A 526 −3.264 53.665 49.960 1.00 25.61 8 4111 CBGLN A 526 −2.101 52.757 47.340 1.00 28.17 6 4112 CG GLN A 526 −2.02853.996 46.486 1.00 30.46 6 4113 CD GLN A 526 −2.542 53.744 45.055 1.0028.73 6 4114 OE1 GLN A 526 −3.419 54.518 44.679 1.00 33.21 8 4115 NE2GLN A 526 −1.951 52.750 44.438 1.00 31.17 7 4116 N GLY A 527 −1.47655.032 49.820 1.00 22.05 7 4117 CA GLY A 527 −2.091 56.150 50.508 1.0020.00 6 4118 C GLY A 527 −2.415 57.258 49.471 1.00 19.58 6 4119 O GLY A527 −2.894 56.897 48.405 1.00 21.95 8 4120 N THR A 528 −2.136 58.50649.804 1.00 21.30 7 4121 CA THR A 528 −2.428 59.597 48.884 1.00 18.42 64122 C THR A 528 −1.268 60.584 48.808 1.00 21.48 6 4123 O THR A 528−0.375 60.642 49.647 1.00 20.31 8 4124 CB THR A 528 −3.685 60.387 49.3201.00 24.98 6 4125 OG1 THR A 528 −3.522 60.782 50.657 1.00 30.73 8 4126CG2 THR A 528 −4.933 59.511 49.240 1.00 26.25 6 4127 N VAL A 529 −1.20961.255 47.667 1.00 16.67 7 4128 CA VAL A 529 −0.167 62.275 47.425 1.0015.19 6 4129 C VAL A 529 −0.924 63.532 46.987 1.00 16.18 6 4130 O VAL A529 −1.825 63.328 46.155 1.00 16.64 8 4131 CB VAL A 529 0.700 61.85146.216 1.00 14.16 6 4132 CG1 VAL A 529 1.664 62.995 45.841 1.00 17.46 64133 CG2 VAL A 529 1.483 60.594 46.604 1.00 18.23 6 4134 N THR A 530−0.533 64.669 47.531 1.00 14.50 7 4135 CA THR A 530 −1.148 65.900 47.0161.00 14.78 6 4136 C THR A 530 −0.038 66.814 46.492 1.00 17.57 6 4137 OTHR A 530 1.076 66.792 47.027 1.00 15.22 8 4138 CB THR A 530 −1.95466.621 48.090 1.00 15.93 6 4139 OG1 THR A 530 −1.209 66.722 49.308 1.0017.69 8 4140 CG2 THR A 530 −3.279 65.858 48.340 1.00 17.39 6 4141 N PHEA 531 −0.395 67.691 45.569 1.00 14.04 7 4142 CA PHE A 531 0.458 68.82245.142 1.00 13.01 6 4143 C PHE A 531 −0.344 70.073 45.496 1.00 15.03 64144 O PHE A 531 −1.454 70.292 44.989 1.00 16.16 8 4145 CB PHE A 5310.659 68.823 43.604 1.00 13.87 6 4146 CG PHE A 531 1.611 67.777 43.0401.00 13.21 6 4147 CD1 PHE A 531 1.438 66.431 43.191 1.00 14.34 6 4148CD2 PHE A 531 2.662 68.228 42.240 1.00 14.96 6 4149 CE1 PHE A 531 2.28865.515 42.629 1.00 16.70 6 4150 CE2 PHE A 531 3.545 67.306 41.691 1.0013.81 6 4151 CZ PHE A 531 3.385 65.943 41.836 1.00 16.70 6 4152 N GLY A532 0.118 70.806 46.490 1.00 14.18 7 4153 CA GLY A 532 −0.569 72.07746.884 1.00 15.57 6 4154 C GLY A 532 −1.992 71.702 47.378 1.00 19.88 64155 O GLY A 532 −2.928 72.482 47.068 1.00 18.91 8 4156 N GLY A 533−2.193 70.510 47.921 1.00 17.41 7 4157 CA GLY A 533 −3.524 70.089 48.4001.00 18.31 6 4158 C GLY A 533 −4.368 69.372 47.370 1.00 20.08 6 4159 OGLY A 533 −5.463 68.817 47.637 1.00 19.31 8 4160 N VAL A 534 −3.92369.391 46.097 1.00 16.06 7 4161 CA VAL A 534 −4.592 68.721 44.999 1.0015.11 6 4162 C VAL A 534 −4.197 67.275 44.894 1.00 15.67 6 4163 O VAL A534 −3.019 66.888 44.712 1.00 17.94 8 4164 CB VAL A 534 −4.368 69.48043.645 1.00 13.67 6 4165 CG1 VAL A 534 −5.101 68.739 42.509 1.00 15.45 64166 CG2 VAL A 534 −4.807 70.937 43.768 1.00 16.93 6 4167 N THR A 535−5.185 66.334 44.967 1.00 13.93 7 4168 CA THR A 535 −4.827 64.927 44.8901.00 16.87 6 4169 C THR A 535 −4.271 64.521 43.536 1.00 20.28 6 4170 OTHR A 535 −4.796 64.893 42.462 1.00 17.64 8 4171 CB THR A 535 −6.06564.042 45.192 1.00 20.23 6 4172 OG1 THR A 535 −6.446 64.284 46.576 1.0020.94 8 4173 CG2 THR A 535 −5.787 62.565 45.026 1.00 24.73 6 4174 N ALAA 536 −3.162 63.773 43.562 1.00 15.87 7 4175 CA ALA A 536 −2.521 63.32442.337 1.00 17.27 6 4176 C ALA A 536 −2.808 61.859 42.042 1.00 20.29 64177 O ALA A 536 −2.929 61.111 43.030 1.00 20.32 8 4178 CB ALA A 536−0.976 63.441 42.384 1.00 17.03 6 4179 N THR A 537 −2.937 61.461 40.7911.00 16.03 7 4180 CA THR A 537 −3.151 60.043 40.489 1.00 15.38 6 4181 CTHR A 537 −1.865 59.242 40.679 1.00 19.21 6 4182 O THR A 537 −0.82359.697 40.166 1.00 19.02 8 4183 CB THR A 537 −3.564 59.955 38.998 1.0018.90 6 4184 OG1 THR A 537 −4.828 60.651 38.950 1.00 19.30 8 4185 CG2THR A 537 −3.697 58.508 38.591 1.00 18.81 6 4186 N VAL A 538 −1.92558.176 41.415 1.00 16.51 7 4187 CA VAL A 538 −0.704 57.394 41.746 1.0016.38 6 4188 C VAL A 538 −0.516 56.415 40.613 1.00 18.34 6 4189 O VAL A538 −1.390 55.599 40.252 1.00 20.80 8 4190 CB VAL A 538 −0.896 56.66543.080 1.00 17.97 6 4191 CG1 VAL A 538 0.219 55.621 43.337 1.00 16.03 64192 CG2 VAL A 538 −1.016 57.646 44.226 1.00 19.59 6 4193 N LYS A 5390.696 56.340 40.055 1.00 15.64 7 4194 CA LYS A 539 1.119 55.341 39.1081.00 14.97 6 4195 C LYS A 539 1.626 54.044 39.732 1.00 17.57 6 4196 OLYS A 539 1.313 52.885 39.375 1.00 18.05 8 4197 CB LYS A 539 2.26455.914 38.209 1.00 17.15 6 4198 CG LYS A 539 2.814 54.859 37.246 1.0020.63 6 4199 CD LYS A 539 3.860 55.636 36.368 1.00 25.39 6 4200 CE LYS A539 3.601 55.199 34.949 1.00 41.98 6 4201 NZ LYS A 539 4.369 53.97634.672 1.00 30.47 7 4202 N SER A 540 2.424 54.212 40.787 1.00 15.53 74203 CA SER A 540 2.919 53.073 41.587 1.00 16.52 6 4204 C SER A 5403.231 53.502 42.999 1.00 17.69 6 4205 O SER A 540 3.482 54.680 43.3061.00 16.82 8 4206 CB SER A 540 4.136 52.424 40.903 1.00 20.58 6 4207 OGSER A 540 5.270 53.317 41.043 1.00 19.05 8 4208 N TRP A 541 3.206 52.53643.953 1.00 16.64 7 4209 CA TRP A 541 3.361 52.905 45.378 1.00 15.40 64210 C TRP A 541 4.148 51.785 46.053 1.00 20.16 6 4211 O TRP A 541 3.68250.647 46.008 1.00 21.11 8 4212 CB TRP A 541 2.034 53.084 46.101 1.0017.49 6 4213 CG TRP A 541 2.124 53.605 47.502 1.00 15.27 6 4214 CD1 TRPA 541 2.645 52.924 48.584 1.00 18.64 6 4215 CD2 TRP A 541 1.689 54.85448.006 1.00 15.30 6 4216 NE1 TRP A 541 2.542 53.673 49.715 1.00 19.85 74217 CE2 TRP A 541 1.976 54.894 49.381 1.00 17.27 6 4218 CE3 TRP A 5411.086 55.984 47.440 1.00 15.92 6 4219 CZ2 TRP A 541 1.703 55.983 50.2011.00 18.49 6 4220 CZ3 TRP A 541 0.787 57.054 48.223 1.00 19.66 6 4221CH2 TRP A 541 1.076 57.063 49.619 1.00 21.41 6 4222 N THR A 542 5.29752.107 46.615 1.00 18.77 7 4223 CA THR A 542 6.111 51.224 47.437 1.0020.27 6 4224 C THR A 542 6.477 51.972 48.690 1.00 21.74 6 4225 O THR A542 6.369 53.228 48.814 1.00 17.27 8 4226 CB THR A 542 7.356 50.64146.743 1.00 24.92 6 4227 OG1 THR A 542 8.305 51.745 46.576 1.00 21.04 84228 CG2 THR A 542 7.091 49.930 45.442 1.00 26.69 6 4229 N SER A 5437.123 51.252 49.648 1.00 18.34 7 4230 CA SER A 543 7.474 51.808 50.9231.00 18.96 6 4231 C SER A 543 8.463 52.975 50.734 1.00 17.37 6 4232 OSER A 543 8.525 53.808 51.615 1.00 19.43 8 4233 CB SER A 543 8.20150.711 51.743 1.00 24.79 6 4234 OG SER A 543 7.254 49.673 51.954 1.0038.42 8 4235 N ASN A 544 9.313 52.865 49.721 1.00 17.78 7 4236 CA ASN A544 10.349 53.917 49.575 1.00 14.67 6 4237 C ASN A 544 10.208 54.72348.287 1.00 15.24 6 4238 O ASN A 544 11.018 55.668 48.072 1.00 16.63 84239 CB AASN A 544 11.734 53.252 49.583 0.50 18.64 6 4240 CG AASN A 54412.145 52.868 51.005 0.50 24.93 6 4241 OD1 AASN A 544 11.394 53.02451.976 0.50 27.01 8 4242 ND2 AASN A 544 13.359 52.364 51.118 0.50 19.547 4240 CB BASN A 544 11.746 53.263 49.523 0.50 15.95 6 4241 CG BASN A544 11.998 52.552 50.860 0.50 20.57 6 4242 OD1 BASN A 544 12.195 53.20551.884 0.50 23.06 8 4243 ND2 BASN A 544 11.914 51.250 50.767 0.50 19.167 4243 N ARG A 545 9.224 54.409 47.426 1.00 14.40 7 4244 CA ARG A 5459.193 55.190 46.167 1.00 16.44 6 4245 C ARG A 545 7.727 55.246 45.6821.00 19.39 6 4246 O ARG A 545 7.083 54.204 45.539 1.00 17.25 8 4247 CBARG A 545 10.085 54.589 45.084 1.00 17.96 6 4248 CG ARG A 545 9.96455.404 43.794 1.00 17.03 6 4249 CD ARG A 545 10.778 54.728 42.653 1.0015.55 6 4250 NE ARG A 545 12.186 54.934 43.045 1.00 17.92 7 4251 CZ ARGA 545 13.164 54.094 42.735 1.00 27.70 6 4252 NH1 ARG A 545 12.923 53.02041.999 1.00 26.35 7 4253 NH2 ARG A 545 14.392 54.343 43.179 1.00 26.80 74254 N ILE A 546 7.282 56.458 45.332 1.00 18.00 7 4255 CA ILE A 5465.908 56.613 44.793 1.00 14.23 6 4256 C ILE A 546 6.077 57.267 43.4061.00 17.86 6 4257 O ILE A 546 6.771 58.296 43.389 1.00 15.62 8 4258 CBILE A 546 5.039 57.498 45.668 1.00 13.38 6 4259 CG1 ILE A 546 4.89556.781 47.045 1.00 15.14 6 4260 CG2 ILE A 546 3.624 57.682 45.030 1.0014.12 6 4261 CD1 ILE A 546 4.473 57.773 48.119 1.00 13.44 6 4262 N GLU A547 5.424 56.777 42.400 1.00 14.74 7 4263 CA GLU A 547 5.338 57.54341.134 1.00 14.58 6 4264 C GLU A 547 3.943 58.116 40.945 1.00 15.30 64265 O GLU A 547 2.977 57.405 41.270 1.00 15.50 8 4266 CB GLU A 5475.537 56.644 39.913 1.00 14.75 6 4267 CG GLU A 547 6.987 56.074 39.8901.00 17.63 6 4268 CD GLU A 547 7.105 55.058 38.781 1.00 21.54 6 4269 OE1GLU A 547 6.335 54.046 38.730 1.00 18.28 8 4270 OE2 GLU A 547 7.92455.225 37.834 1.00 16.92 8 4271 N VAL A 548 3.865 59.377 40.603 1.0012.67 7 4272 CA VAL A 548 2.565 60.033 40.428 1.00 13.16 6 4273 C VAL A548 2.565 60.764 39.095 1.00 15.52 6 4274 O VAL A 548 3.587 61.02838.477 1.00 14.55 8 4275 CB VAL A 548 2.266 61.100 41.499 1.00 15.22 64276 CG1 VAL A 548 2.134 60.409 42.872 1.00 17.06 6 4277 CG2 VAL A 5483.376 62.179 41.584 1.00 16.26 6 4278 N TYR A 549 1.338 61.119 38.6441.00 12.92 7 4279 CA TYR A 549 1.226 61.997 37.481 1.00 14.43 6 4280 CTYR A 549 0.902 63.397 37.975 1.00 13.16 6 4281 O TYR A 549 0.223 63.57139.016 1.00 14.84 8 4282 CB TYR A 549 0.000 61.611 36.605 1.00 14.89 64283 CG TYR A 549 0.208 60.240 36.037 1.00 14.21 6 4284 CD1 TYR A 5491.049 60.058 34.934 1.00 17.04 6 4285 CD2 TYR A 549 −0.398 59.160 36.6281.00 14.96 6 4286 CE1 TYR A 549 1.252 58.788 34.395 1.00 19.51 6 4287CE2 TYR A 549 −0.214 57.885 36.081 1.00 20.11 6 4288 CZ TYR A 549 0.57757.730 34.984 1.00 20.28 6 4289 OH TYR A 549 0.789 56.436 34.508 1.0021.51 8 4290 N VAL A 550 1.626 64.446 37.496 1.00 12.41 7 4291 CA VAL A550 1.317 65.794 37.957 1.00 13.30 6 4292 C VAL A 550 −0.145 66.13937.602 1.00 12.86 6 4293 O VAL A 550 −0.589 65.893 36.503 1.00 15.42 84294 CB VAL A 550 2.195 66.791 37.131 1.00 12.38 6 4295 CG1 VAL A 5501.968 68.236 37.581 1.00 13.91 6 4296 CG2 VAL A 550 3.657 66.404 37.5421.00 16.31 6 4297 N PRO A 551 −0.828 66.685 38.603 1.00 13.48 7 4298 CAPRO A 551 −2.272 66.942 38.387 1.00 16.42 6 4299 C PRO A 551 −2.44768.081 37.424 1.00 16.09 6 4300 O PRO A 551 −1.599 68.955 37.236 1.0016.43 8 4301 CB PRO A 551 −2.869 67.337 39.755 1.00 20.53 6 4302 CG PROA 551 −1.772 66.991 40.707 1.00 20.55 6 4303 CD PRO A 551 −0.427 66.84939.973 1.00 17.00 6 4304 N ASN A 552 −3.658 68.150 36.821 1.00 15.47 74305 CA ASN A 552 −4.017 69.248 35.941 1.00 15.18 6 4306 C ASN A 552−4.401 70.475 36.748 1.00 19.54 6 4307 O ASN A 552 −5.630 70.744 36.9171.00 19.65 8 4308 CB ASN A 552 −5.198 68.759 35.075 1.00 19.00 6 4309 CGASN A 552 −5.522 69.706 33.925 1.00 23.61 6 4310 OD1 ASN A 552 −4.76370.583 33.553 1.00 29.14 8 4311 ND2 ASN A 552 −6.635 69.481 33.239 1.0023.65 7 4312 N MET A 553 −3.487 71.146 37.402 1.00 13.46 7 4313 CA MET A553 −3.722 72.208 38.346 1.00 11.50 6 4314 C MET A 553 −3.003 73.45637.901 1.00 15.54 6 4315 O MET A 553 −2.319 73.427 36.881 1.00 17.61 84316 CB MET A 553 −3.328 71.835 39.803 1.00 16.46 6 4317 CG MET A 553−1.826 71.490 39.883 1.00 14.92 6 4318 SD MET A 553 −1.364 70.962 41.5791.00 17.71 16 4319 CE MET A 553 −1.416 72.450 42.426 1.00 16.59 6 4320 NALA A 554 −3.278 74.532 38.619 1.00 17.19 7 4321 CA ALA A 554 −2.71175.834 38.289 1.00 21.10 6 4322 C ALA A 554 −1.169 75.788 38.321 1.0017.79 6 4323 O ALA A 554 −0.631 75.032 39.141 1.00 17.24 8 4324 CB ALA A554 −3.075 76.757 39.471 1.00 24.10 6 4325 N ALA A 555 −0.537 76.59137.500 1.00 14.57 7 4326 CA ALA A 555 0.947 76.567 37.489 1.00 13.27 64327 C ALA A 555 1.568 77.356 38.600 1.00 13.78 6 4328 O ALA A 555 1.05178.305 39.204 1.00 14.85 8 4329 CB ALA A 555 1.375 77.200 36.142 1.0016.26 6 4330 N GLY A 556 2.874 76.966 38.857 1.00 12.02 7 4331 CA GLY A556 3.602 77.675 39.947 1.00 14.17 6 4332 C GLY A 556 4.312 76.63940.815 1.00 12.79 6 4333 O GLY A 556 4.121 75.415 40.670 1.00 12.92 84334 N LEU A 557 5.203 77.130 41.670 1.00 14.81 7 4335 CA LEU A 5575.876 76.232 42.626 1.00 13.54 6 4336 C LEU A 557 4.918 75.806 43.7371.00 12.41 6 4337 O LEU A 557 4.110 76.659 44.188 1.00 14.95 8 4338 CBLEU A 557 7.091 76.999 43.221 1.00 13.41 6 4339 CG LEU A 557 8.01876.123 44.069 1.00 15.11 6 4340 CD1 LEU A 557 8.847 75.220 43.141 1.0013.33 6 4341 CD2 LEU A 557 8.965 77.046 44.898 1.00 17.39 6 4342 N THR A558 4.801 74.500 43.858 1.00 13.24 7 4343 CA THR A 558 3.807 73.94144.818 1.00 13.26 6 4344 C THR A 558 4.469 72.927 45.741 1.00 16.19 64345 O THR A 558 5.520 72.402 45.379 1.00 16.82 8 4346 CB THR A 5582.616 73.378 44.044 1.00 17.75 6 4347 OG1 THR A 558 1.566 73.153 45.0101.00 18.46 8 4348 CG2 THR A 558 2.886 72.099 43.320 1.00 14.65 6 4349 NASP A 559 3.750 72.559 46.821 1.00 13.53 7 4350 CA ASP A 559 4.35171.569 47.739 1.00 13.26 6 4351 C ASP A 559 3.718 70.202 47.564 1.0017.40 6 4352 O ASP A 559 2.469 70.015 47.579 1.00 17.26 8 4353 CB ASP A559 4.129 72.027 49.195 1.00 13.77 6 4354 CG ASP A 559 4.998 73.21949.580 1.00 25.94 6 4355 OD1 ASP A 559 6.174 73.267 49.201 1.00 23.88 84356 OD2 ASP A 559 4.468 74.127 50.251 1.00 28.55 8 4357 N VAL A 5604.576 69.205 47.465 1.00 12.44 7 4358 CA VAL A 560 4.161 67.801 47.3921.00 11.28 6 4359 C VAL A 560 4.193 67.207 48.826 1.00 14.98 6 4360 OVAL A 560 5.085 67.470 49.616 1.00 15.44 8 4361 CB VAL A 560 5.14466.953 46.555 1.00 11.93 6 4362 CG1 VAL A 560 4.738 65.496 46.488 1.0016.58 6 4363 CG2 VAL A 560 5.186 67.516 45.122 1.00 14.73 6 4364 N LYS A561 3.136 66.439 49.097 1.00 15.49 7 4365 CA LYS A 561 2.989 65.83550.443 1.00 14.90 6 4366 C LYS A 561 2.427 64.452 50.269 1.00 15.23 64367 O LYS A 561 1.502 64.157 49.522 1.00 16.90 8 4368 CB LYS A 5611.960 66.720 51.206 1.00 18.50 6 4369 CG LYS A 561 1.847 66.177 52.6561.00 22.42 6 4370 CD LYS A 561 1.025 67.110 53.523 1.00 25.69 6 4371 CELYS A 561 −0.461 66.912 53.312 1.00 33.13 6 4372 NZ LYS A 561 −1.19868.004 54.033 1.00 37.04 7 4373 N VAL A 562 2.947 63.489 51.047 1.0016.07 7 4374 CA VAL A 562 2.525 62.108 51.051 1.00 14.01 6 4375 C VAL A562 1.751 61.827 52.382 1.00 14.81 6 4376 O VAL A 562 2.150 62.32453.398 1.00 17.73 8 4377 CB VAL A 562 3.735 61.158 51.036 1.00 16.60 64378 CG1 VAL A 562 3.312 59.677 51.185 1.00 16.48 6 4379 CG2 VAL A 5624.473 61.228 49.672 1.00 17.80 6 4380 N THR A 563 0.603 61.156 52.1401.00 17.67 7 4381 CA THR A 563 −0.181 60.806 53.380 1.00 18.18 6 4382 CTHR A 563 −0.261 59.308 53.412 1.00 18.30 6 4383 O THR A 563 −0.67958.642 52.456 1.00 19.93 8 4384 CB THR A 563 −1.542 61.496 53.361 1.0018.11 6 4385 OG1 THR A 563 −1.367 62.891 53.406 1.00 19.44 8 4386 CG2THR A 563 −2.281 61.112 54.705 1.00 20.36 6 4387 N ALA A 564 0.15458.701 54.548 1.00 21.05 7 4388 CA ALA A 564 0.245 57.258 54.649 1.0024.26 6 4389 C ALA A 564 −0.234 56.845 56.060 1.00 23.28 6 4390 O ALA A564 0.104 57.536 57.008 1.00 21.58 8 4391 CB ALA A 564 1.658 56.71154.437 1.00 25.03 6 4392 N GLY A 565 −1.218 55.968 56.140 1.00 30.08 74393 CA GLY A 565 −1.857 55.701 57.443 1.00 31.09 6 4394 C GLY A 565−2.488 56.887 58.121 1.00 35.06 6 4395 O GLY A 565 −2.493 56.983 59.3631.00 31.36 8 4396 N GLY A 566 −3.025 57.873 57.403 1.00 32.22 7 4397 CAGLY A 566 −3.549 59.083 58.011 1.00 31.70 6 4398 C GLY A 566 −2.52360.107 58.438 1.00 31.07 6 4399 O GLY A 566 −2.936 61.213 58.829 1.0032.69 8 4400 N VAL A 567 −1.202 59.887 58.271 1.00 26.17 7 4401 CA VAL A567 −0.186 60.798 58.776 1.00 21.45 6 4402 C VAL A 567 0.537 61.48857.557 1.00 17.95 6 4403 O VAL A 567 0.692 60.707 56.658 1.00 18.75 84404 CB VAL A 567 0.945 60.023 59.500 1.00 26.89 6 4405 CG1 VAL A 5671.981 60.946 60.096 1.00 30.00 6 4406 CG2 VAL A 567 0.308 59.088 60.5671.00 33.86 6 4407 N SER A 568 0.687 62.774 57.699 1.00 19.77 7 4408 CASER A 568 1.267 63.410 56.486 1.00 19.16 6 4409 C SER A 568 2.770 63.58556.688 1.00 19.28 6 4410 O SER A 568 3.351 63.752 57.763 1.00 21.35 84411 CB SER A 568 0.574 64.705 56.156 1.00 29.69 6 4412 OG SER A 5680.595 65.549 57.266 1.00 41.18 8 4413 N SER A 569 3.399 63.581 55.5031.00 19.22 7 4414 CA SER A 569 4.867 63.784 55.480 1.00 17.43 6 4415 CSER A 569 5.229 65.245 55.568 1.00 17.17 6 4416 O SER A 569 4.519 66.26655.502 1.00 17.53 8 4417 CB SER A 569 5.381 63.220 54.137 1.00 17.58 64418 OG SER A 569 5.066 64.083 53.025 1.00 15.50 8 4419 N ASN A 5706.572 65.473 55.538 1.00 14.77 7 4420 CA ASN A 570 7.143 66.776 55.2531.00 13.84 6 4421 C ASN A 570 6.848 67.107 53.752 1.00 13.33 6 4422 OASN A 570 6.527 66.217 52.996 1.00 16.50 8 4423 CB ASN A 570 8.67066.723 55.435 1.00 17.22 6 4424 CG ASN A 570 9.363 65.581 54.758 1.0016.95 6 4425 OD1 ASN A 570 9.038 64.399 54.745 1.00 15.12 8 4426 ND2 ASNA 570 10.455 65.853 54.023 1.00 16.51 7 4427 N LEU A 571 7.108 68.38153.486 1.00 14.82 7 4428 CA LEU A 571 6.705 68.878 52.131 1.00 12.49 64429 C LEU A 571 7.959 69.019 51.282 1.00 15.87 6 4430 O LEU A 571 9.02469.355 51.828 1.00 16.79 8 4431 CB LEU A 571 6.147 70.286 52.340 1.0015.18 6 4432 CG LEU A 571 4.911 70.396 53.250 1.00 22.77 6 4433 CD1 LEUA 571 4.368 71.807 53.300 1.00 22.26 6 4434 CD2 LEU A 571 3.834 69.44852.757 1.00 22.04 6 4435 N TYR A 572 7.747 68.878 49.946 1.00 13.65 74436 CA TYR A 572 8.930 69.100 49.067 1.00 12.87 6 4437 C TYR A 5728.322 69.878 47.880 1.00 14.52 6 4438 O TYR A 572 7.347 69.399 47.2621.00 14.71 8 4439 CB TYR A 572 9.480 67.704 48.701 1.00 12.62 6 4440 CGTYR A 572 10.887 67.679 48.121 1.00 13.61 6 4441 CD1 TYR A 572 11.07968.175 46.835 1.00 13.57 6 4442 CD2 TYR A 572 11.946 67.161 48.845 1.0015.40 6 4443 CE1 TYR A 572 12.361 68.168 46.257 1.00 13.80 6 4444 CE2TYR A 572 13.221 67.135 48.283 1.00 12.70 6 4445 CZ TYR A 572 13.40067.629 47.002 1.00 14.33 6 4446 OH TYR A 572 14.710 67.607 46.466 1.0013.40 8 4447 N SER A 573 9.060 70.874 47.387 1.00 13.37 7 4448 CA SER A573 8.571 71.734 46.294 1.00 12.21 6 4449 C SER A 573 8.665 71.05544.920 1.00 12.75 6 4450 O SER A 573 9.520 70.234 44.703 1.00 12.64 84451 CB ASER A 573 9.436 72.999 46.162 0.60 17.33 6 4452 OG ASER A 5739.459 73.767 47.331 0.60 22.77 8 4452 CB BSER A 573 9.408 73.025 46.2760.40 15.40 6 4453 OG BSER A 573 10.793 72.728 46.149 0.40 16.17 8 4453 NTYR A 574 7.838 71.568 44.000 1.00 11.56 7 4454 CA TYR A 574 7.91271.077 42.604 1.00 10.89 6 4455 C TYR A 574 7.374 72.249 41.771 1.0013.28 6 4456 O TYR A 574 6.344 72.860 42.138 1.00 12.17 8 4457 CB TYR A574 7.041 69.857 42.405 1.00 11.94 6 4458 CG TYR A 574 6.917 69.37940.971 1.00 11.37 6 4459 CD1 TYR A 574 7.921 68.521 40.467 1.00 12.69 64460 CD2 TYR A 574 5.867 69.781 40.162 1.00 11.85 6 4461 CE1 TYR A 5747.863 68.052 39.154 1.00 13.23 6 4462 CE2 TYR A 574 5.792 69.313 38.8341.00 13.93 6 4463 CZ TYR A 574 6.796 68.466 38.366 1.00 11.32 6 4464 OHTYR A 574 6.679 68.006 37.078 1.00 12.54 8 4465 N ASN A 575 7.992 72.51040.627 1.00 12.18 7 4466 CA ASN A 575 7.578 73.682 39.820 1.00 12.18 64467 C ASN A 575 6.738 73.306 38.608 1.00 12.59 6 4468 O ASN A 575 7.17172.699 37.598 1.00 12.20 8 4469 CB ASN A 575 8.898 74.351 39.331 1.0012.02 6 4470 CG ASN A 575 8.635 75.707 38.700 1.00 17.00 6 4471 OD1 ASNA 575 7.562 76.292 38.872 1.00 14.54 8 4472 ND2 ASN A 575 9.608 76.22337.934 1.00 13.02 7 4473 N ILE A 576 5.400 73.515 38.739 1.00 10.95 74474 CA ILE A 576 4.506 73.221 37.604 1.00 10.36 6 4475 C ILE A 5764.485 74.374 36.602 1.00 12.05 6 4476 O ILE A 576 4.145 75.497 36.9301.00 13.39 8 4477 CB ILE A 576 3.036 73.061 38.127 1.00 12.95 6 4478 CG1ILE A 576 3.082 71.956 39.190 1.00 13.10 6 4479 CG2 ILE A 576 2.07972.677 36.966 1.00 14.18 6 4480 CD1 ILE A 576 1.709 71.488 39.691 1.0015.07 6 4481 N LEU A 577 4.883 74.054 35.368 1.00 10.51 7 4482 CA LEU A577 4.908 75.052 34.303 1.00 12.74 6 4483 C LEU A 577 3.480 75.30833.772 1.00 11.80 6 4484 O LEU A 577 2.572 74.474 34.021 1.00 13.37 84485 CB LEU A 577 5.757 74.463 33.137 1.00 11.48 6 4486 CG LEU A 5777.226 74.238 33.569 1.00 12.21 6 4487 CD1 LEU A 577 7.982 73.601 32.4211.00 13.03 6 4488 CD2 LEU A 577 7.897 75.576 33.989 1.00 13.85 6 4489 NSER A 578 3.398 76.385 33.006 1.00 11.76 7 4490 CA SER A 578 2.03776.726 32.475 1.00 15.00 6 4491 C SER A 578 1.681 75.960 31.215 1.0017.37 6 4492 O SER A 578 0.553 76.134 30.685 1.00 17.93 8 4493 CB SER A578 2.081 78.230 32.132 1.00 13.25 6 4494 OG SER A 578 2.321 78.96733.305 1.00 14.45 8 4495 N GLY A 579 2.538 75.095 30.688 1.00 15.28 74496 CA GLY A 579 2.266 74.270 29.497 1.00 14.88 6 4497 C GLY A 5793.627 74.010 28.818 1.00 13.39 6 4498 O GLY A 579 4.670 74.450 29.3181.00 14.78 8 4499 N THR A 580 3.518 73.227 27.740 1.00 11.35 7 4500 CATHR A 580 4.803 72.961 27.005 1.00 13.16 6 4501 C THR A 580 5.419 74.29226.647 1.00 14.61 6 4502 O THR A 580 4.747 75.282 26.349 1.00 14.26 84503 CB THR A 580 4.517 72.009 25.835 1.00 13.57 6 4504 OG1 THR A 5805.753 71.676 25.176 1.00 16.06 8 4505 CG2 THR A 580 3.688 72.715 24.7321.00 20.75 6 4506 N GLN A 581 6.787 74.346 26.706 1.00 11.89 7 4507 CAGLN A 581 7.454 75.658 26.609 1.00 10.06 6 4508 C GLN A 581 8.012 75.90525.148 1.00 10.19 6 4509 O GLN A 581 8.163 75.020 24.338 1.00 12.94 84510 CB GLN A 581 8.751 75.601 27.465 1.00 11.27 6 4511 CG GLN A 5818.407 75.301 28.975 1.00 10.49 6 4512 CD GLN A 581 7.920 76.579 29.6541.00 12.45 6 4513 OE1 GLN A 581 8.545 77.588 29.921 1.00 13.44 8 4514NE2 GLN A 581 6.582 76.528 30.002 1.00 11.11 7 4515 N THR A 582 8.20277.209 24.953 1.00 9.52 7 4516 CA THR A 582 8.978 77.646 23.772 1.0010.13 6 4517 C THR A 582 10.049 78.609 24.293 1.00 10.70 6 4518 O THR A582 9.921 79.235 25.313 1.00 12.73 8 4519 CB THR A 582 8.018 78.30622.763 1.00 12.88 6 4520 OG1 THR A 582 8.736 78.798 21.599 1.00 12.92 84521 CG2 THR A 582 7.265 79.504 23.359 1.00 11.55 6 4522 N SER A 58311.166 78.712 23.507 1.00 11.67 7 4523 CA SER A 583 12.321 79.527 23.9311.00 12.58 6 4524 C SER A 583 12.300 80.783 23.061 1.00 11.58 6 4525 OSER A 583 12.496 80.687 21.844 1.00 12.44 8 4526 CB SER A 583 13.61278.697 23.747 1.00 12.53 6 4527 OG SER A 583 14.755 79.449 24.240 1.0014.73 8 4528 N VAL A 584 12.118 81.899 23.781 1.00 10.19 7 4529 CA VAL A584 11.741 83.141 23.016 1.00 9.76 6 4530 C VAL A 584 12.721 84.26823.298 1.00 11.27 6 4531 O VAL A 584 13.066 84.570 24.440 1.00 11.87 84532 CB VAL A 584 10.358 83.645 23.506 1.00 12.33 6 4533 CG1 VAL A 58410.041 84.968 22.757 1.00 14.53 6 4534 CG2 VAL A 584 9.279 82.604 23.2201.00 12.71 6 4535 N VAL A 585 13.307 84.868 22.244 1.00 10.77 7 4536 CAVAL A 585 14.166 86.030 22.421 1.00 9.69 6 4537 C VAL A 585 13.24487.219 22.693 1.00 12.06 6 4538 O VAL A 585 12.450 87.576 21.803 1.0014.60 8 4539 CB VAL A 585 14.882 86.310 21.064 1.00 11.53 6 4540 CG1 VALA 585 15.712 87.605 21.158 1.00 15.03 6 4541 CG2 VAL A 585 15.750 85.11120.717 1.00 14.67 6 4542 N PHE A 586 13.361 87.762 23.908 1.00 12.32 74543 CA PHE A 586 12.622 88.986 24.243 1.00 12.19 6 4544 C PHE A 58613.584 90.161 24.063 1.00 14.77 6 4545 O PHE A 586 14.668 90.209 24.7091.00 12.38 8 4546 CB PHE A 586 12.174 88.944 25.704 1.00 12.57 6 4547 CGPHE A 586 10.886 88.184 25.987 1.00 11.39 6 4548 CD1 PHE A 586 10.87986.809 26.009 1.00 13.56 6 4549 CD2 PHE A 586 9.694 88.868 26.231 1.0013.70 6 4550 CE1 PHE A 586 9.758 86.060 26.284 1.00 13.86 6 4551 CE2 PHEA 586 8.543 88.102 26.520 1.00 12.32 6 4552 CZ PHE A 586 8.577 86.70726.558 1.00 11.70 6 4553 N THR A 587 13.189 91.146 23.239 1.00 14.16 74554 CA THR A 587 14.016 92.324 23.066 1.00 12.96 6 4555 C THR A 58713.247 93.561 23.468 1.00 13.58 6 4556 O THR A 587 12.072 93.651 23.0581.00 15.22 8 4557 CB THR A 587 14.421 92.464 21.555 1.00 11.66 6 4558OG1 THR A 587 15.145 91.299 21.141 1.00 15.06 8 4559 CG2 THR A 58715.331 93.708 21.318 1.00 13.37 6 4560 N VAL A 588 13.829 94.487 24.1951.00 14.03 7 4561 CA VAL A 588 13.156 95.779 24.469 1.00 14.79 6 4562 CVAL A 588 14.079 96.867 23.912 1.00 14.40 6 4563 O VAL A 588 15.25897.015 24.225 1.00 15.56 8 4564 CB VAL A 588 12.863 95.933 25.971 1.0014.24 6 4565 CG1 VAL A 588 14.111 95.935 26.870 1.00 14.60 6 4566 CG2VAL A 588 12.079 97.255 26.232 1.00 13.38 6 4567 N LYS A 589 13.47897.570 22.915 1.00 15.39 7 4568 CA LYS A 589 14.212 98.670 22.258 1.0016.20 6 4569 C LYS A 589 14.180 100.009 22.953 1.00 18.01 6 4570 O LYS A589 13.230 100.355 23.652 1.00 15.39 8 4571 CB LYS A 589 13.597 98.82020.860 1.00 16.23 6 4572 CG LYS A 589 13.908 97.588 20.008 1.00 17.01 64573 CD LYS A 589 13.275 97.825 18.634 1.00 24.71 6 4574 CE LYS A 58913.494 96.582 17.792 1.00 37.49 6 4575 NZ LYS A 589 13.368 96.852 16.3211.00 51.36 7 4576 N SER A 590 15.302 100.747 22.828 1.00 16.34 7 4577 CASER A 590 15.371 102.116 23.293 1.00 19.32 6 4578 C SER A 590 15.006102.295 24.746 1.00 19.68 6 4579 O SER A 590 14.185 103.146 25.151 1.0017.24 8 4580 CB SER A 590 14.448 103.009 22.421 1.00 20.32 6 4581 OG SERA 590 14.867 102.933 21.046 1.00 22.81 8 4582 N ALA A 591 15.698 101.51425.612 1.00 17.08 7 4583 CA ALA A 591 15.458 101.617 27.048 1.00 16.02 64584 C ALA A 591 16.178 102.871 27.530 1.00 18.06 6 4585 O ALA A 59117.152 103.325 26.878 1.00 15.85 8 4586 CB ALA A 591 16.045 100.32627.695 1.00 15.17 6 4587 N PRO A 592 15.872 103.303 28.730 1.00 18.28 74588 CA PRO A 592 16.493 104.529 29.298 1.00 18.18 6 4589 C PRO A 59217.967 104.319 29.512 1.00 22.69 6 4590 O PRO A 592 18.463 103.18029.693 1.00 19.12 8 4591 CB PRO A 592 15.762 104.797 30.621 1.00 19.23 64592 CG PRO A 592 14.433 104.085 30.387 1.00 23.18 6 4593 CD PRO A 59214.795 102.833 29.585 1.00 17.71 6 4594 N PRO A 593 18.778 105.36729.550 1.00 21.02 7 4595 CA PRO A 593 20.204 105.252 29.779 1.00 20.83 64596 C PRO A 593 20.494 104.537 31.094 1.00 20.17 6 4597 O PRO A 59319.811 104.784 32.102 1.00 21.50 8 4598 CB PRO A 593 20.715 106.72729.941 1.00 22.70 6 4599 CG PRO A 593 19.643 107.491 29.165 1.00 24.71 64600 CD PRO A 593 18.337 106.774 29.432 1.00 23.44 6 4601 N THR A 59421.530 103.723 31.165 1.00 19.91 7 4602 CA THR A 594 21.909 103.06032.402 1.00 21.78 6 4603 C THR A 594 23.380 103.366 32.686 1.00 23.13 64604 O THR A 594 24.138 103.737 31.787 1.00 23.96 8 4605 CB THR A 59421.729 101.521 32.292 1.00 23.27 6 4606 OG1 THR A 594 22.466 101.09431.140 1.00 20.06 8 4607 CG2 THR A 594 20.245 101.183 32.157 1.00 21.336 4608 N ASN A 595 23.764 103.210 33.928 1.00 23.96 7 4609 CA ASN A 59525.142 103.193 34.370 1.00 28.93 6 4610 C ASN A 595 25.614 101.79134.716 1.00 31.88 6 4611 O ASN A 595 24.847 100.849 34.915 1.00 22.74 84612 CB ASN A 595 25.285 104.099 35.620 1.00 34.82 6 4613 CG ASN A 59524.970 105.532 35.180 1.00 36.76 6 4614 OD1 ASN A 595 24.047 106.19035.647 1.00 42.57 8 4615 ND2 ASN A 595 25.738 106.004 34.208 1.00 38.167 4616 N LEU A 596 26.939 101.654 34.839 1.00 34.83 7 4617 CA LEU A 59627.559 100.380 35.212 1.00 37.55 6 4618 C LEU A 596 26.947 99.803 36.4881.00 31.76 6 4619 O LEU A 596 26.589 100.502 37.435 1.00 35.49 8 4620 CBLEU A 596 29.051 100.642 35.407 1.00 48.79 6 4621 CG LEU A 596 30.04299.528 35.681 1.00 52.60 6 4622 CD1 LEU A 596 29.894 98.971 37.092 1.0056.16 6 4623 CD2 LEU A 596 29.934 98.433 34.628 1.00 56.63 6 4624 N GLYA 597 26.492 98.556 36.348 1.00 30.34 7 4625 CA GLY A 597 25.861 97.86037.473 1.00 30.50 6 4626 C GLY A 597 24.337 97.822 37.288 1.00 25.20 64627 O GLY A 597 23.705 96.996 37.949 1.00 23.57 8 4628 N ASP A 59823.780 98.803 36.544 1.00 21.92 7 4629 CA ASP A 598 22.315 98.799 36.3991.00 18.64 6 4630 C ASP A 598 21.982 97.666 35.429 1.00 21.53 6 4631 OASP A 598 22.702 97.563 34.399 1.00 20.69 8 4632 CB ASP A 598 21.814100.096 35.763 1.00 17.61 6 4633 CG ASP A 598 22.046 101.382 36.536 1.0020.17 6 4634 OD1 ASP A 598 22.364 101.347 37.751 1.00 19.25 8 4635 OD2ASP A 598 21.858 102.432 35.868 1.00 22.20 8 4636 N LYS A 599 20.86196.919 35.612 1.00 18.66 7 4637 CA LYS A 599 20.593 95.891 34.605 1.0015.76 6 4638 C LYS A 599 19.056 95.824 34.461 1.00 11.90 6 4639 O LYS A599 18.320 96.237 35.358 1.00 19.04 8 4640 CB LYS A 599 21.049 94.48435.006 1.00 23.86 6 4641 CG LYS A 599 22.597 94.419 35.031 1.00 25.32 64642 CD LYS A 599 23.118 93.007 35.252 1.00 26.43 6 4643 CE LYS A 59924.656 93.063 35.120 1.00 32.43 6 4644 NZ LYS A 599 25.179 91.656 35.1061.00 35.89 7 4645 N ILE A 600 18.623 95.442 33.287 1.00 13.51 7 4646 CAILE A 600 17.178 95.336 33.021 1.00 12.20 6 4647 C ILE A 600 16.74693.886 33.130 1.00 13.74 6 4648 O ILE A 600 17.476 92.927 32.799 1.0014.24 8 4649 CB ILE A 600 16.938 95.829 31.554 1.00 13.87 6 4650 CG1 ILEA 600 17.249 97.335 31.566 1.00 21.52 6 4651 CG2 ILE A 600 15.499 95.61831.051 1.00 15.85 6 4652 CD1 ILE A 600 16.798 98.104 30.313 1.00 23.52 64653 N TYR A 601 15.545 93.745 33.676 1.00 13.09 7 4654 CA TYR A 60114.926 92.453 33.883 1.00 12.76 6 4655 C TYR A 601 13.531 92.475 33.2881.00 13.27 6 4656 O TYR A 601 12.914 93.491 32.986 1.00 15.09 8 4657 CBTYR A 601 14.751 92.119 35.387 1.00 14.11 6 4658 CG TYR A 601 16.06591.805 36.078 1.00 11.98 6 4659 CD1 TYR A 601 16.902 92.834 36.502 1.0012.52 6 4660 CD2 TYR A 601 16.473 90.490 36.242 1.00 12.95 6 4661 CE1TYR A 601 18.138 92.544 37.097 1.00 13.54 6 4662 CE2 TYR A 601 17.67390.213 36.888 1.00 14.26 6 4663 CZ TYR A 601 18.499 91.239 37.276 1.0015.84 6 4664 OH TYR A 601 19.691 90.903 37.935 1.00 16.92 8 4665 N LEU A602 12.986 91.285 33.068 1.00 11.99 7 4666 CA LEU A 602 11.657 91.05732.494 1.00 13.20 6 4667 C LEU A 602 10.762 90.434 33.580 1.00 14.26 64668 O LEU A 602 11.148 89.522 34.284 1.00 13.06 8 4669 CB LEU A 60211.794 90.060 31.334 1.00 13.29 6 4670 CG LEU A 602 10.506 89.432 30.8001.00 10.59 6 4671 CD1 LEU A 602 9.579 90.481 30.155 1.00 14.08 6 4672CD2 LEU A 602 10.864 88.385 29.704 1.00 11.83 6 4673 N THR A 603 9.48290.861 33.649 1.00 12.02 7 4674 CA THR A 603 8.570 90.233 34.635 1.0012.81 6 4675 C THR A 603 7.158 90.267 34.066 1.00 12.50 6 4676 O THR A603 6.876 91.096 33.183 1.00 14.59 8 4677 CB THR A 603 8.711 90.98335.969 1.00 14.38 6 4678 OG1 THR A 603 7.971 90.241 36.987 1.00 14.53 84679 CG2 THR A 603 8.152 92.414 35.971 1.00 15.35 6 4680 N GLY A 6046.310 89.331 34.489 1.00 11.51 7 4681 CA GLY A 604 4.995 89.274 33.7871.00 11.82 6 4682 C GLY A 604 4.042 88.348 34.530 1.00 12.03 6 4683 OGLY A 604 4.358 87.909 35.636 1.00 13.68 8 4684 N ASN A 605 2.911 88.08233.859 1.00 12.03 7 4685 CA ASN A 605 1.782 87.516 34.637 1.00 11.85 64686 C ASN A 605 1.680 86.017 34.575 1.00 12.50 6 4687 O ASN A 605 0.61585.441 34.625 1.00 14.07 8 4688 CB ASN A 605 0.481 88.161 34.031 1.0013.77 6 4689 CG ASN A 605 0.265 87.610 32.629 1.00 17.19 6 4690 OD1 ASNA 605 1.080 87.101 31.828 1.00 13.63 8 4691 ND2 ASN A 605 −1.025 87.68132.165 1.00 16.36 7 4692 N ILE A 606 2.823 85.308 34.560 1.00 13.26 74693 CA ILE A 606 2.836 83.860 34.628 1.00 11.73 6 4694 C ILE A 6064.099 83.493 35.448 1.00 13.02 6 4695 O ILE A 606 5.005 84.349 35.5111.00 13.34 8 4696 CB ILE A 606 2.995 83.184 33.259 1.00 11.81 6 4697 CG1ILE A 606 4.029 83.874 32.346 1.00 12.94 6 4698 CG2 ILE A 606 1.62583.138 32.550 1.00 15.56 6 4699 CD1 ILE A 606 4.300 82.981 31.113 1.0015.13 6 4700 N PRO A 607 4.181 82.331 36.033 1.00 13.09 7 4701 CA PRO A607 5.294 81.982 36.937 1.00 12.68 6 4702 C PRO A 607 6.616 81.88036.189 1.00 10.98 6 4703 O PRO A 607 7.700 82.258 36.671 1.00 14.73 84704 CB PRO A 607 4.895 80.647 37.607 1.00 13.69 6 4705 CG PRO A 6073.818 80.118 36.675 1.00 16.48 6 4706 CD PRO A 607 3.081 81.335 36.0981.00 16.43 6 4707 N GLU A 608 6.531 81.525 34.880 1.00 11.74 7 4708 CAGLU A 608 7.747 81.559 34.031 1.00 10.58 6 4709 C GLU A 608 8.382 82.95833.994 1.00 13.60 6 4710 O GLU A 608 9.606 83.060 33.731 1.00 11.79 84711 CB GLU A 608 7.437 81.056 32.616 1.00 11.09 6 4712 CG GLU A 6087.145 79.550 32.522 1.00 10.94 6 4713 CD GLU A 608 5.674 79.163 32.6991.00 14.31 6 4714 OE1 GLU A 608 4.875 79.973 33.221 1.00 12.87 8 4715OE2 GLU A 608 5.344 78.040 32.280 1.00 13.22 8 4716 N LEU A 609 7.57183.999 34.112 1.00 11.31 7 4717 CA LEU A 609 8.093 85.359 34.095 1.0011.00 6 4718 C LEU A 609 7.944 86.002 35.453 1.00 12.01 6 4719 O LEU A609 7.959 87.224 35.602 1.00 14.24 8 4720 CB LEU A 609 7.249 86.18833.078 1.00 14.30 6 4721 CG LEU A 609 7.424 85.668 31.627 1.00 13.57 64722 CD1 LEU A 609 6.672 86.643 30.695 1.00 18.28 6 4723 CD2 LEU A 6098.912 85.648 31.238 1.00 14.71 6 4724 N GLY A 610 7.854 85.194 36.5251.00 10.78 7 4725 CA GLY A 610 7.950 85.729 37.864 1.00 10.94 6 4726 CGLY A 610 6.664 86.230 38.554 1.00 13.37 6 4727 O GLY A 610 6.767 86.83239.647 1.00 13.90 8 4728 N ASN A 611 5.525 86.174 37.906 1.00 13.56 74729 CA ASN A 611 4.262 86.696 38.463 1.00 14.13 6 4730 C ASN A 6114.462 88.079 39.072 1.00 13.68 6 4731 O ASN A 611 4.063 88.427 40.2071.00 14.78 8 4732 CB ASN A 611 3.695 85.782 39.555 1.00 13.73 6 4733 CGASN A 611 3.110 84.538 38.890 1.00 16.98 6 4734 OD1 ASN A 611 2.35384.585 37.897 1.00 17.26 8 4735 ND2 ASN A 611 3.501 83.420 39.478 1.0016.08 7 4736 N TRP A 612 5.010 88.962 38.242 1.00 13.00 7 4737 CA TRP A612 5.298 90.339 38.534 1.00 13.35 6 4738 C TRP A 612 6.284 90.67639.608 1.00 14.25 6 4739 O TRP A 612 6.420 91.775 40.107 1.00 15.26 84740 CB TRP A 612 3.915 91.044 38.832 1.00 13.65 6 4741 CG TRP A 6122.965 91.036 37.664 1.00 13.25 6 4742 CD1 TRP A 612 1.775 90.359 37.6321.00 13.84 6 4743 CD2 TRP A 612 3.138 91.564 36.359 1.00 14.07 6 4744NE1 TRP A 612 1.160 90.489 36.402 1.00 13.90 7 4745 CE2 TRP A 612 1.98391.288 35.617 1.00 16.64 6 4746 CE3 TRP A 612 4.148 92.402 35.815 1.0015.91 6 4747 CZ2 TRP A 612 1.843 91.676 34.288 1.00 14.35 6 4748 CZ3 TRPA 612 3.980 92.856 34.506 1.00 14.55 6 4749 CH2 TRP A 612 2.844 92.49033.747 1.00 14.05 6 4750 N SER A 613 7.114 89.674 40.049 1.00 14.59 74751 CA SER A 613 8.136 89.943 41.025 1.00 16.76 6 4752 C SER A 6139.171 90.916 40.471 1.00 15.94 6 4753 O SER A 613 9.510 90.841 39.2811.00 15.44 8 4754 CB SER A 613 8.804 88.572 41.315 1.00 14.15 6 4755 OGSER A 613 9.842 88.719 42.250 1.00 15.35 8 4756 N THR A 614 9.821 91.64841.406 1.00 13.40 7 4757 CA THR A 614 11.021 92.394 41.037 1.00 13.18 64758 C THR A 614 12.238 91.869 41.796 1.00 12.85 6 4759 O THR A 61413.311 92.464 41.777 1.00 15.88 8 4760 CB THR A 614 10.895 93.904 41.2971.00 16.41 6 4761 OG1 THR A 614 10.626 94.073 42.724 1.00 18.07 8 4762CG2 THR A 614 9.718 94.523 40.520 1.00 18.09 6 4763 N ASP A 615 12.03390.680 42.425 1.00 13.65 7 4764 CA ASP A 615 13.138 90.024 43.143 1.0015.24 6 4765 C ASP A 615 14.084 89.416 42.093 1.00 12.74 6 4766 O ASP A615 13.582 88.794 41.143 1.00 13.71 8 4767 CB ASP A 615 12.511 88.98144.075 1.00 14.77 6 4768 CG ASP A 615 13.634 88.423 44.970 1.00 21.15 64769 OD1 ASP A 615 13.956 88.932 46.048 1.00 23.65 8 4770 OD2 ASP A 61514.204 87.431 44.586 1.00 18.42 8 4771 N THR A 616 15.390 89.536 42.3501.00 12.77 7 4772 CA THR A 616 16.387 89.067 41.365 1.00 13.57 6 4773 CTHR A 616 17.391 88.146 42.072 1.00 15.88 6 4774 O THR A 616 18.48787.902 41.566 1.00 14.89 8 4775 CB THR A 616 17.144 90.224 40.674 1.0014.32 6 4776 OG1 THR A 616 17.752 91.045 41.713 1.00 15.99 8 4777 CG2THR A 616 16.189 91.128 39.884 1.00 16.33 6 4778 N SER A 617 16.98187.590 43.216 1.00 13.15 7 4779 CA SER A 617 17.813 86.641 43.956 1.0012.49 6 4780 C SER A 617 17.759 85.265 43.312 1.00 13.68 6 4781 O SER A617 17.193 85.034 42.235 1.00 12.79 8 4782 CB SER A 617 17.271 86.58345.396 1.00 14.38 6 4783 OG SER A 617 16.056 85.882 45.441 1.00 15.10 84784 N GLY A 618 18.327 84.268 44.080 1.00 15.05 7 4785 CA GLY A 61818.300 82.869 43.621 1.00 13.01 6 4786 C GLY A 618 16.967 82.147 43.8111.00 13.49 6 4787 O GLY A 618 16.835 80.938 43.552 1.00 15.47 8 4788 NALA A 619 15.893 82.847 44.200 1.00 13.99 7 4789 CA ALA A 619 14.59282.218 44.333 1.00 14.93 6 4790 C ALA A 619 14.033 81.691 43.015 1.0015.28 6 4791 O ALA A 619 14.489 82.043 41.907 1.00 15.28 8 4792 CB ALA A619 13.582 83.263 44.854 1.00 17.52 6 4793 N VAL A 620 13.043 80.80543.172 1.00 11.74 7 4794 CA VAL A 620 12.419 80.230 41.967 1.00 12.25 64795 C VAL A 620 11.259 81.126 41.502 1.00 12.14 6 4796 O VAL A 62010.533 81.679 42.344 1.00 14.38 8 4797 CB VAL A 620 11.796 78.892 42.4361.00 15.46 6 4798 CG1 VAL A 620 11.242 78.231 41.173 1.00 13.86 6 4799CG2 VAL A 620 12.924 77.941 42.923 1.00 15.04 6 4800 N ASN A 621 11.15781.254 40.168 1.00 12.23 7 4801 CA ASN A 621 10.066 82.044 39.571 1.0012.45 6 4802 C ASN A 621 9.968 83.484 40.032 1.00 12.62 6 4803 O ASN A621 8.860 83.896 40.480 1.00 12.87 8 4804 CB ASN A 621 8.676 81.34639.732 1.00 10.99 6 4805 CG ASN A 621 8.656 79.972 39.084 1.00 11.13 64806 OD1 ASN A 621 9.398 79.689 38.141 1.00 13.90 8 4807 ND2 ASN A 6217.742 79.105 39.596 1.00 13.32 7 4808 N ASN A 622 11.106 84.199 40.0481.00 13.97 7 4809 CA ASN A 622 11.116 85.623 40.322 1.00 11.35 6 4810 CASN A 622 11.418 86.389 39.037 1.00 12.47 6 4811 O ASN A 622 11.09085.862 37.960 1.00 12.66 8 4812 CB ASN A 622 12.073 85.956 41.471 1.0012.54 6 4813 CG ASN A 622 13.543 85.545 41.151 1.00 12.82 6 4814 OD1 ASNA 622 13.811 85.093 40.044 1.00 12.70 8 4815 ND2 ASN A 622 14.377 85.75342.196 1.00 13.72 7 4816 N ALA A 623 11.883 87.626 39.098 1.00 11.27 74817 CA ALA A 623 12.088 88.339 37.812 1.00 12.38 6 4818 C ALA A 62313.107 87.592 36.947 1.00 13.25 6 4819 O ALA A 623 14.035 87.018 37.4691.00 13.43 8 4820 CB ALA A 623 12.586 89.748 38.120 1.00 14.46 6 4821 NGLN A 624 12.905 87.740 35.631 1.00 12.11 7 4822 CA GLN A 624 13.74287.034 34.660 1.00 11.87 6 4823 C GLN A 624 14.828 87.912 34.071 1.0012.70 6 4824 O GLN A 624 14.646 89.092 33.762 1.00 13.14 8 4825 CB GLN A624 12.880 86.477 33.521 1.00 14.55 6 4826 CG GLN A 624 11.779 85.49234.084 1.00 13.33 6 4827 CD GLN A 624 12.451 84.323 34.754 1.00 14.35 64828 OE1 GLN A 624 13.213 83.546 34.096 1.00 15.81 8 4829 NE2 GLN A 62412.268 84.078 36.040 1.00 14.08 7 4830 N GLY A 625 15.989 87.264 33.9411.00 12.93 7 4831 CA GLY A 625 17.183 87.950 33.418 1.00 12.61 6 4832 CGLY A 625 18.392 87.917 34.310 1.00 12.24 6 4833 O GLY A 625 18.49786.888 34.934 1.00 13.82 8 4834 N PRO A 626 19.296 88.815 34.131 1.0012.81 7 4835 CA PRO A 626 19.237 90.097 33.510 1.00 15.64 6 4836 C PRO A626 19.288 89.998 32.003 1.00 15.42 6 4837 O PRO A 626 19.675 88.99231.364 1.00 15.65 8 4838 CB PRO A 626 20.374 91.012 34.019 1.00 15.71 64839 CG PRO A 626 21.401 89.927 34.320 1.00 14.63 6 4840 CD PRO A 62620.565 88.780 34.858 1.00 13.83 6 4841 N LEU A 627 18.725 91.061 31.3321.00 13.98 7 4842 CA LEU A 627 18.935 91.116 29.881 1.00 13.16 6 4843 CLEU A 627 20.364 91.609 29.649 1.00 14.14 6 4844 O LEU A 627 21.02492.215 30.527 1.00 14.86 8 4845 CB LEU A 627 17.906 92.080 29.214 1.0013.73 6 4846 CG LEU A 627 16.549 91.433 28.919 1.00 13.68 6 4847 CD1 LEUA 627 15.771 91.075 30.200 1.00 16.08 6 4848 CD2 LEU A 627 15.630 92.37028.084 1.00 16.33 6 4849 N LEU A 628 20.804 91.374 28.421 1.00 12.55 74850 CA LEU A 628 22.139 91.805 27.919 1.00 12.76 6 4851 C LEU A 62821.994 92.999 26.973 1.00 15.67 6 4852 O LEU A 628 20.910 93.197 26.3941.00 14.76 8 4853 CB LEU A 628 22.746 90.663 27.111 1.00 14.06 6 4854 CGLEU A 628 22.848 89.332 27.886 1.00 14.72 6 4855 CD1 LEU A 628 23.52688.239 27.056 1.00 12.14 6 4856 CD2 LEU A 628 23.659 89.508 29.185 1.0020.12 6 4857 N ALA A 629 23.117 93.699 26.702 1.00 16.33 7 4858 CA ALA A629 22.871 94.875 25.787 1.00 16.83 6 4859 C ALA A 629 23.983 95.08324.795 1.00 15.77 6 4860 O ALA A 629 24.610 96.177 24.707 1.00 15.92 84861 CB ALA A 629 22.674 96.098 26.674 1.00 19.56 6 4862 N PRO A 63024.278 94.136 23.970 1.00 16.96 7 4863 CA PRO A 630 25.237 94.281 22.8731.00 19.28 6 4864 C PRO A 630 24.773 95.400 21.940 1.00 21.06 6 4865 OPRO A 630 25.633 96.015 21.314 1.00 23.58 8 4866 CB PRO A 630 25.31492.944 22.123 1.00 17.59 6 4867 CG PRO A 630 23.928 92.367 22.442 1.0018.42 6 4868 CD PRO A 630 23.644 92.807 23.877 1.00 18.05 6 4869 N ASN A631 23.464 95.562 21.768 1.00 17.93 7 4870 CA ASN A 631 22.935 96.63520.926 1.00 17.58 6 4871 C ASN A 631 22.382 97.779 21.748 1.00 17.45 64872 O ASN A 631 21.359 98.370 21.354 1.00 18.41 8 4873 CB ASN A 63121.902 96.082 19.950 1.00 18.61 6 4874 CG ASN A 631 22.400 94.876 19.1611.00 28.21 6 4875 OD1 ASN A 631 21.838 93.764 19.168 1.00 27.73 8 4876ND2 ASN A 631 23.476 95.224 18.455 1.00 19.54 7 4877 N TYR A 632 22.98098.110 22.883 1.00 16.27 7 4878 CA TYR A 632 22.570 99.229 23.700 1.0017.84 6 4879 C TYR A 632 22.255 100.496 22.909 1.00 19.89 6 4880 O TYR A632 23.030 100.672 21.982 1.00 19.89 8 4881 CB TYR A 632 23.749 99.53724.643 1.00 18.23 6 4882 CG TYR A 632 23.520 100.604 25.654 1.00 20.78 64883 CD1 TYR A 632 22.919 100.369 26.875 1.00 20.07 6 4884 CD2 TYR A 63223.839 101.933 25.333 1.00 22.98 6 4885 CE1 TYR A 632 22.700 101.36727.797 1.00 22.62 6 4886 CE2 TYR A 632 23.578 102.953 26.223 1.00 23.646 4887 CZ TYR A 632 23.051 102.671 27.457 1.00 27.32 6 4888 OH TYR A 63222.814 103.670 28.369 1.00 23.27 8 4889 N PRO A 633 21.113 101.06723.157 1.00 19.06 7 4890 CA PRO A 633 20.194 101.103 24.225 1.00 16.58 64891 C PRO A 633 19.087 100.033 24.123 1.00 15.76 6 4892 O PRO A 63318.188 100.153 24.954 1.00 16.24 8 4893 CB PRO A 633 19.474 102.49824.311 1.00 19.94 6 4894 CG PRO A 633 19.449 102.810 22.846 1.00 24.00 64895 CD PRO A 633 20.772 102.271 22.369 1.00 24.76 6 4896 N ASP A 63419.272 99.094 23.169 1.00 16.18 7 4897 CA ASP A 634 18.330 97.978 23.1211.00 16.48 6 4898 C ASP A 634 18.923 96.792 23.937 1.00 15.97 6 4899 OASP A 634 20.153 96.671 24.058 1.00 16.27 8 4900 CB ASP A 634 18.13397.402 21.731 1.00 15.05 6 4901 CG ASP A 634 17.626 98.434 20.695 1.0020.07 6 4902 OD1 ASP A 634 17.138 99.519 21.100 1.00 17.34 8 4903 OD2ASP A 634 17.728 98.097 19.503 1.00 19.32 8 4904 N TRP A 635 18.00996.147 24.656 1.00 14.45 7 4905 CA TRP A 635 18.413 95.017 25.510 1.0016.15 6 4906 C TRP A 635 17.708 93.736 25.082 1.00 13.84 6 4907 O TRP A635 16.590 93.820 24.606 1.00 13.90 8 4908 CB TRP A 635 18.024 95.29926.962 1.00 15.52 6 4909 CG TRP A 635 18.818 96.421 27.587 1.00 14.07 64910 CD1 TRP A 635 18.737 97.739 27.178 1.00 14.13 6 4911 CD2 TRP A 63519.713 96.407 28.694 1.00 16.17 6 4912 NE1 TRP A 635 19.561 98.53327.989 1.00 15.61 7 4913 CE2 TRP A 635 20.179 97.706 28.908 1.00 17.77 64914 CE3 TRP A 635 20.179 95.350 29.511 1.00 18.51 6 4915 CZ2 TRP A 63521.071 98.018 29.935 1.00 19.26 6 4916 CZ3 TRP A 635 21.100 95.67130.515 1.00 23.17 6 4917 CH2 TRP A 635 21.514 96.992 30.735 1.00 20.92 64918 N PHE A 636 18.294 92.561 25.372 1.00 12.41 7 4919 CA PHE A 63617.562 91.335 24.947 1.00 11.57 6 4920 C PHE A 636 18.071 90.194 25.8551.00 12.41 6 4921 O PHE A 636 19.204 90.239 26.345 1.00 13.24 8 4922 CBPHE A 636 17.761 90.971 23.435 1.00 12.03 6 4923 CG PHE A 636 19.03090.118 23.261 1.00 12.15 6 4924 CD1 PHE A 636 20.287 90.667 23.292 1.0017.38 6 4925 CD2 PHE A 636 18.856 88.751 23.095 1.00 11.02 6 4926 CE1PHE A 636 21.417 89.860 23.207 1.00 19.56 6 4927 CE2 PHE A 636 19.99687.906 22.997 1.00 12.49 6 4928 CZ PHE A 636 21.250 88.466 23.034 1.0017.21 6 4929 N TYR A 637 17.229 89.170 25.966 1.00 12.09 7 4930 CA TYR A637 17.759 87.841 26.425 1.00 12.35 6 4931 C TYR A 637 16.714 86.84825.989 1.00 12.24 6 4932 O TYR A 637 15.911 87.135 25.088 1.00 12.49 84933 CB TYR A 637 18.183 87.770 27.903 1.00 12.77 6 4934 CG TYR A 63719.035 86.513 28.195 1.00 13.33 6 4935 CD1 TYR A 637 20.253 86.24427.548 1.00 12.60 6 4936 CD2 TYR A 637 18.595 85.573 29.127 1.00 10.55 64937 CE1 TYR A 637 21.022 85.134 27.792 1.00 11.85 6 4938 CE2 TYR A 63719.321 84.424 29.387 1.00 12.60 6 4939 CZ TYR A 637 20.521 84.221 28.7281.00 11.69 6 4940 OH TYR A 637 21.255 83.073 29.016 1.00 11.85 8 4941 NVAL A 638 16.857 85.565 26.379 1.00 12.66 7 4942 CA VAL A 638 16.03384.508 25.827 1.00 10.90 6 4943 C VAL A 638 15.492 83.693 27.023 1.0011.04 6 4944 O VAL A 638 16.202 83.367 27.980 1.00 13.35 8 4945 CB VAL A638 16.830 83.496 24.987 1.00 12.00 6 4946 CG1 VAL A 638 15.922 82.65024.118 1.00 12.74 6 4947 CG2 VAL A 638 17.799 84.300 24.074 1.00 10.59 64948 N PHE A 639 14.137 83.517 26.957 1.00 12.77 7 4949 CA PHE A 63913.441 82.960 28.082 1.00 9.34 6 4950 C PHE A 639 12.466 81.877 27.6651.00 11.56 6 4951 O PHE A 639 11.814 81.982 26.632 1.00 12.26 8 4952 CBPHE A 639 12.612 84.072 28.807 1.00 11.50 6 4953 CG PHE A 639 13.49885.209 29.322 1.00 12.29 6 4954 CD1 PHE A 639 14.294 85.042 30.446 1.0011.38 6 4955 CD2 PHE A 639 13.567 86.380 28.563 1.00 13.67 6 4956 CE1PHE A 639 15.176 86.094 30.829 1.00 12.05 6 4957 CE2 PHE A 639 14.41687.425 28.965 1.00 13.84 6 4958 CZ PHE A 639 15.196 87.301 30.113 1.0013.28 6 4959 N SER A 640 12.323 80.913 28.609 1.00 10.61 7 4960 CA SER A640 11.376 79.833 28.360 1.00 11.72 6 4961 C SER A 640 10.005 80.22328.872 1.00 11.19 6 4962 O SER A 640 9.878 80.649 30.026 1.00 12.90 84963 CB SER A 640 11.915 78.568 29.132 1.00 12.23 6 4964 OG SER A 64011.028 77.448 28.846 1.00 12.04 8 4965 N VAL A 641 9.007 80.190 27.9751.00 8.82 7 4966 CA VAL A 641 7.635 80.609 28.374 1.00 11.37 6 4967 CVAL A 641 6.697 79.601 27.775 1.00 11.35 6 4968 O VAL A 641 7.075 78.84026.864 1.00 10.31 8 4969 CB VAL A 641 7.286 82.019 27.760 1.00 11.50 64970 CG1 VAL A 641 8.061 83.038 28.624 1.00 13.20 6 4971 CG2 VAL A 6417.607 82.115 26.241 1.00 10.82 6 4972 N PRO A 642 5.470 79.384 28.2541.00 10.92 7 4973 CA PRO A 642 4.582 78.438 27.626 1.00 11.56 6 4974 CPRO A 642 4.256 78.780 26.166 1.00 10.87 6 4975 O PRO A 642 4.048 79.99425.888 1.00 12.26 8 4976 CB PRO A 642 3.295 78.524 28.529 1.00 11.37 64977 CG PRO A 642 3.352 79.948 29.064 1.00 11.52 6 4978 CD PRO A 6424.866 80.234 29.308 1.00 14.12 6 4979 N ALA A 643 4.267 77.800 25.2911.00 11.34 7 4980 CA ALA A 643 4.033 77.992 23.839 1.00 12.12 6 4981 CALA A 643 2.531 78.215 23.567 1.00 13.78 6 4982 O ALA A 643 1.681 77.65024.236 1.00 15.31 8 4983 CB ALA A 643 4.330 76.657 23.141 1.00 13.71 64984 N GLY A 644 2.317 79.106 22.623 1.00 14.27 7 4985 CA GLY A 6440.952 79.377 22.150 1.00 14.42 6 4986 C GLY A 644 0.065 80.108 23.1331.00 15.94 6 4987 O GLY A 644 −1.154 79.765 23.178 1.00 19.30 8 4988 NLYS A 645 0.597 80.884 24.030 1.00 14.60 7 4989 CA LYS A 645 −0.17181.519 25.092 1.00 14.20 6 4990 C LYS A 645 −0.060 83.017 24.926 1.0017.57 6 4991 O LYS A 645 1.002 83.579 24.623 1.00 17.47 8 4992 CB LYS A645 0.376 81.126 26.483 1.00 14.57 6 4993 CG LYS A 645 0.313 79.61126.725 1.00 17.45 6 4994 CD LYS A 645 −1.136 79.116 26.699 1.00 17.54 64995 CE LYS A 645 −1.184 77.572 26.837 1.00 21.69 6 4996 NZ LYS A 645−0.587 77.121 28.112 1.00 31.91 7 4997 N THR A 646 −1.157 83.717 25.3571.00 14.42 7 4998 CA THR A 646 −1.090 85.140 25.434 1.00 14.66 6 4999 CTHR A 646 −0.662 85.594 26.824 1.00 13.55 6 5000 O THR A 646 −1.22185.157 27.850 1.00 16.55 8 5001 CB THR A 646 −2.510 85.720 25.098 1.0017.00 6 5002 OG1 THR A 646 −2.824 85.361 23.738 1.00 16.76 8 5003 CG2THR A 646 −2.463 87.240 25.195 1.00 18.18 6 5004 N ILE A 647 0.36086.434 26.913 1.00 11.81 7 5005 CA ILE A 647 1.001 86.816 28.152 1.0011.47 6 5006 C ILE A 647 1.047 88.357 28.250 1.00 13.84 6 5007 O ILE A647 0.991 89.054 27.201 1.00 14.89 8 5008 CB ILE A 647 2.476 86.35328.278 1.00 13.09 6 5009 CG1 ILE A 647 3.296 86.770 27.045 1.00 12.50 65010 CG2 ILE A 647 2.410 84.817 28.343 1.00 14.24 6 5011 CD1 ILE A 6474.813 86.486 27.247 1.00 17.78 6 5012 N GLN A 648 1.150 88.776 29.4951.00 12.61 7 5013 CA GLN A 648 1.402 90.212 29.726 1.00 11.91 6 5014 CGLN A 648 2.687 90.407 30.490 1.00 15.15 6 5015 O GLN A 648 3.041 89.58631.338 1.00 15.89 8 5016 CB GLN A 648 0.298 90.835 30.611 1.00 13.04 65017 CG GLN A 648 −1.032 90.704 29.820 1.00 20.15 6 5018 CD GLN A 648−2.040 91.727 30.260 1.00 27.13 6 5019 OE1 GLN A 648 −1.797 92.69130.982 1.00 23.22 8 5020 NE2 GLN A 648 −3.309 91.503 29.847 1.00 28.35 75021 N PHE A 649 3.446 91.461 30.155 1.00 13.26 7 5022 CA PHE A 6494.767 91.622 30.746 1.00 12.72 6 5023 C PHE A 649 5.219 93.094 30.6631.00 14.64 6 5024 O PHE A 649 4.697 93.903 29.862 1.00 14.50 8 5025 CBPHE A 649 5.812 90.743 30.051 1.00 12.47 6 5026 CG PHE A 649 5.87590.962 28.544 1.00 13.33 6 5027 CD1 PHE A 649 4.996 90.400 27.682 1.0014.84 6 5028 CD2 PHE A 649 6.861 91.790 28.013 1.00 13.41 6 5029 CE1 PHEA 649 5.031 90.678 26.303 1.00 15.17 6 5030 CE2 PHE A 649 6.977 92.04326.666 1.00 16.16 6 5031 CZ PHE A 649 6.057 91.493 25.807 1.00 13.88 65032 N LYS A 650 6.135 93.413 31.538 1.00 13.99 7 5033 CA LYS A 6506.876 94.683 31.405 1.00 13.18 6 5034 C LYS A 650 8.349 94.411 31.7971.00 15.87 6 5035 O LYS A 650 8.696 93.364 32.375 1.00 13.96 8 5036 CBLYS A 650 6.358 95.735 32.410 1.00 14.62 6 5037 CG LYS A 650 5.00496.385 31.989 1.00 15.36 6 5038 CD LYS A 650 4.922 97.604 32.979 1.0019.44 6 5039 CE LYS A 650 3.841 98.565 32.553 1.00 24.45 6 5040 NZ LYS A650 3.898 99.741 33.515 1.00 18.41 7 5041 N PHE A 651 9.172 95.39831.438 1.00 13.40 7 5042 CA PHE A 651 10.571 95.420 31.850 1.00 14.23 65043 C PHE A 651 10.800 96.474 32.926 1.00 16.48 6 5044 O PHE A 6519.990 97.396 33.132 1.00 17.07 8 5045 CB PHE A 651 11.465 95.783 30.6381.00 12.48 6 5046 CG PHE A 651 11.280 94.796 29.512 1.00 15.91 6 5047CD1 PHE A 651 10.277 94.943 28.564 1.00 13.76 6 5048 CD2 PHE A 65112.127 93.681 29.453 1.00 14.89 6 5049 CE1 PHE A 651 10.114 94.01627.568 1.00 12.48 6 5050 CE2 PHE A 651 11.957 92.759 28.426 1.00 13.50 65051 CZ PHE A 651 10.944 92.884 27.461 1.00 16.56 6 5052 N PHE A 65211.849 96.240 33.723 1.00 15.18 7 5053 CA PHE A 652 12.249 97.256 34.7041.00 14.29 6 5054 C PHE A 652 13.756 97.339 34.785 1.00 17.92 6 5055 OPHE A 652 14.452 96.365 34.487 1.00 15.37 8 5056 CB PHE A 652 11.63496.950 36.084 1.00 15.14 6 5057 CG PHE A 652 12.097 95.688 36.789 1.0016.77 6 5058 CD1 PHE A 652 13.251 95.685 37.565 1.00 15.74 6 5059 CD2PHE A 652 11.326 94.553 36.695 1.00 15.90 6 5060 CE1 PHE A 652 13.63394.518 38.231 1.00 14.76 6 5061 CE2 PHE A 652 11.695 93.407 37.380 1.0015.19 6 5062 CZ PHE A 652 12.866 93.343 38.139 1.00 14.25 6 5063 N ILE A653 14.244 98.512 35.189 1.00 14.94 7 5064 CA ILE A 653 15.705 98.59835.463 1.00 14.72 6 5065 C ILE A 653 15.906 98.394 36.962 1.00 18.67 65066 O ILE A 653 15.175 98.971 37.804 1.00 19.59 8 5067 CB ILE A 65316.168 100.071 35.163 1.00 14.73 6 5068 CG1 ILE A 653 16.000 100.33733.693 1.00 18.74 6 5069 CG2 ILE A 653 17.628 100.201 35.616 1.00 18.256 5070 CD1 ILE A 653 16.191 101.838 33.353 1.00 20.43 6 5071 N LYS A 65416.847 97.524 37.282 1.00 17.58 7 5072 CA LYS A 654 17.273 97.382 38.6901.00 18.28 6 5073 C LYS A 654 18.623 98.139 38.780 1.00 15.87 6 5074 OLYS A 654 19.571 97.760 38.135 1.00 18.77 8 5075 CB LYS A 654 17.46995.933 39.131 1.00 16.77 6 5076 CG LYS A 654 17.774 95.976 40.661 1.0020.67 6 5077 CD LYS A 654 17.709 94.558 41.225 1.00 24.12 6 5078 CE LYSA 654 18.152 94.544 42.680 1.00 30.47 6 5079 NZ LYS A 654 17.967 93.15243.221 1.00 39.55 7 5080 N ARG A 655 18.538 99.361 39.337 1.00 19.37 75081 CA ARG A 655 19.776 100.164 39.391 1.00 21.00 6 5082 C ARG A 65520.820 99.478 40.256 1.00 24.58 6 5083 O ARG A 655 20.486 98.604 41.0571.00 22.97 8 5084 CB ARG A 655 19.445 101.531 40.003 1.00 18.71 6 5085CG ARG A 655 18.411 102.323 39.192 1.00 19.26 6 5086 CD ARG A 655 19.036102.699 37.864 1.00 24.72 6 5087 NE ARG A 655 18.169 103.597 37.102 1.0023.26 7 5088 CZ ARG A 655 18.428 104.073 35.883 1.00 23.74 6 5089 NH1ARG A 655 19.508 103.812 35.193 1.00 20.63 7 5090 NH2 ARG A 655 17.509104.882 35.343 1.00 24.30 7 5091 N ALA A 656 22.090 99.900 40.135 1.0024.51 7 5092 CA ALA A 656 23.170 99.305 40.898 1.00 28.24 6 5093 C ALA A656 22.865 99.430 42.401 1.00 27.25 6 5094 O ALA A 656 23.305 98.53343.117 1.00 32.90 8 5095 CB ALA A 656 24.518 100.009 40.656 1.00 29.09 65096 N ASP A 657 22.145 100.427 42.856 1.00 31.34 7 5097 CA ASP A 65721.850 100.561 44.282 1.00 32.95 6 5098 C ASP A 657 20.617 99.783 44.6941.00 33.22 6 5099 O ASP A 657 20.202 99.906 45.852 1.00 30.17 8 5100 CBASP A 657 21.725 102.050 44.643 1.00 27.78 6 5101 CG ASP A 657 20.499102.712 44.087 1.00 34.66 6 5102 OD1 ASP A 657 19.665 102.035 43.4311.00 28.22 8 5103 OD2 ASP A 657 20.239 103.920 44.267 1.00 33.52 8 5104N GLY A 658 20.019 98.958 43.803 1.00 29.54 7 5105 CA GLY A 658 18.87498.181 44.227 1.00 29.70 6 5106 C GLY A 658 17.543 98.837 43.931 1.0026.81 6 5107 O GLY A 658 16.531 98.126 43.935 1.00 30.39 8 5108 N THR A659 17.502 100.106 43.566 1.00 23.52 7 5109 CA THR A 659 16.313 100.82643.215 1.00 25.61 6 5110 C THR A 659 15.641 100.184 41.985 1.00 23.40 65111 O THR A 659 16.419 99.778 41.118 1.00 27.85 8 5112 CB THR A 65916.614 102.279 42.717 1.00 19.42 6 5113 OG1 THR A 659 17.524 102.99343.510 1.00 46.62 8 5114 CG2 THR A 659 15.276 103.016 42.706 1.00 37.026 5115 N ILE A 660 14.319 100.215 41.909 1.00 20.34 7 5116 CA ILE A 66013.596 99.691 40.758 1.00 25.29 6 5117 C ILE A 660 12.933 100.761 39.9191.00 25.57 6 5118 O ILE A 660 12.186 101.612 40.465 1.00 27.02 8 5119 CBILE A 660 12.458 98.722 41.207 1.00 26.69 6 5120 CG1 ILE A 660 13.01297.534 41.991 1.00 27.58 6 5121 CG2 ILE A 660 11.704 98.273 39.972 1.0021.18 6 5122 CD1 ILE A 660 14.022 96.722 41.221 1.00 24.46 6 5123 N GLNA 661 13.169 100.849 38.624 1.00 20.86 7 5124 CA GLN A 661 12.479101.793 37.743 1.00 19.49 6 5125 C GLN A 661 11.720 101.014 36.669 1.0020.02 6 5126 O GLN A 661 12.266 100.405 35.730 1.00 19.24 8 5127 CB GLNA 661 13.410 102.775 37.023 1.00 20.06 6 5128 CG GLN A 661 12.611103.688 36.077 1.00 21.00 6 5129 CD GLN A 661 13.541 104.665 35.350 1.0021.47 6 5130 OE1 GLN A 661 13.279 104.997 34.195 1.00 28.51 8 5131 NE2GLN A 661 14.578 105.095 36.040 1.00 22.67 7 5132 N TRP A 662 10.389100.926 36.834 1.00 20.75 7 5133 CA TRP A 662 9.556 100.227 35.857 1.0018.49 6 5134 C TRP A 662 9.441 100.967 34.536 1.00 21.67 6 5135 O TRP A662 9.412 102.230 34.565 1.00 19.29 8 5136 CB TRP A 662 8.152 100.08236.437 1.00 18.81 6 5137 CG TRP A 662 7.960 99.114 37.551 1.00 18.39 65138 CD1 TRP A 662 8.083 99.359 38.889 1.00 19.35 6 5139 CD2 TRP A 6627.543 97.752 37.419 1.00 18.13 6 5140 NE1 TRP A 662 7.781 98.218 39.6081.00 21.46 7 5141 CE2 TRP A 662 7.444 97.223 38.713 1.00 18.92 6 5142CE3 TRP A 662 7.213 96.960 36.295 1.00 18.78 6 5143 CZ2 TRP A 662 6.99495.923 38.966 1.00 16.39 6 5144 CZ3 TRP A 662 6.798 95.661 36.537 1.0018.67 6 5145 CH2 TRP A 662 6.725 95.156 37.854 1.00 15.44 6 5146 N GLU A663 9.170 100.250 33.453 1.00 18.24 7 5147 CA GLU A 663 8.551 100.85732.292 1.00 17.79 6 5148 C GLU A 663 7.240 101.517 32.740 1.00 17.95 65149 O GLU A 663 6.519 100.973 33.574 1.00 18.49 8 5150 CB GLU A 6638.001 99.880 31.232 1.00 22.54 6 5151 CG GLU A 663 9.065 99.526 30.1951.00 23.03 6 5152 CD GLU A 663 8.380 98.560 29.223 1.00 19.52 6 5153 OE1GLU A 663 8.159 97.397 29.619 1.00 17.12 8 5154 OE2 GLU A 663 8.06398.990 28.102 1.00 18.01 8 5155 N ASN A 664 6.892 102.576 32.027 1.0018.62 7 5156 CA ASN A 664 5.604 103.189 32.365 1.00 18.27 6 5157 C ASN A664 4.522 102.581 31.484 1.00 20.85 6 5158 O ASN A 664 4.782 101.67130.702 1.00 21.34 8 5159 CB ASN A 664 5.790 104.696 32.115 1.00 22.20 65160 CG ASN A 664 6.447 105.326 33.350 1.00 30.00 6 5161 OD1 ASN A 6646.281 104.932 34.519 1.00 35.11 8 5162 ND2 ASN A 664 7.238 106.36633.127 1.00 33.46 7 5163 N GLY A 665 3.295 103.085 31.667 1.00 22.07 75164 CA GLY A 665 2.187 102.708 30.786 1.00 23.10 6 5165 C GLY A 6651.557 101.363 31.102 1.00 21.34 6 5166 O GLY A 665 1.827 100.710 32.1191.00 22.70 8 5167 N SER A 666 0.832 100.839 30.093 1.00 18.43 7 5168 CASER A 666 0.135 99.581 30.305 1.00 17.79 6 5169 C SER A 666 1.084 98.40330.046 1.00 16.94 6 5170 O SER A 666 2.005 98.503 29.261 1.00 16.68 85171 CB SER A 666 −1.037 99.440 29.297 1.00 24.19 6 5172 OG SER A 666−1.959 100.498 29.645 1.00 24.86 8 5173 N ASN A 667 0.642 97.227 30.4701.00 14.27 7 5174 CA ASN A 667 1.491 96.058 30.168 1.00 16.75 6 5175 CASN A 667 1.575 95.824 28.678 1.00 17.00 6 5176 O ASN A 667 0.616 96.05027.899 1.00 15.91 8 5177 CB ASN A 667 0.795 94.804 30.736 1.00 16.66 65178 CG ASN A 667 0.703 94.817 32.248 1.00 19.33 6 5179 OD1 ASN A 667−0.178 94.105 32.855 1.00 20.96 8 5180 ND2 ASN A 667 1.594 95.513 32.8871.00 16.21 7 5181 N HIS A 668 2.720 95.243 28.272 1.00 13.63 7 5182 CAHIS A 668 2.882 94.747 26.930 1.00 15.66 6 5183 C HIS A 668 2.137 93.40826.856 1.00 16.10 6 5184 O HIS A 668 2.048 92.666 27.847 1.00 16.87 85185 CB HIS A 668 4.327 94.431 26.491 1.00 15.51 6 5186 CG HIS A 6685.208 95.653 26.519 1.00 14.13 6 5187 ND1 HIS A 668 5.229 96.451 25.3751.00 15.75 7 5188 CD2 HIS A 668 6.066 96.158 27.410 1.00 17.00 6 5189CE1 HIS A 668 6.108 97.464 25.592 1.00 14.21 6 5190 NE2 HIS A 668 6.58197.305 26.830 1.00 15.51 7 5191 N VAL A 669 1.434 93.208 25.734 1.0015.02 7 5192 CA VAL A 669 0.684 91.987 25.490 1.00 16.94 6 5193 C VAL A669 1.205 91.294 24.260 1.00 14.25 6 5194 O VAL A 669 1.414 91.93623.206 1.00 17.08 8 5195 CB VAL A 669 −0.852 92.295 25.322 1.00 17.60 65196 CG1 VAL A 669 −1.624 90.970 25.253 1.00 20.63 6 5197 CG2 VAL A 669−1.341 93.078 26.547 1.00 17.53 6 5198 N ALA A 670 1.450 89.971 24.2871.00 14.50 7 5199 CA ALA A 670 1.945 89.249 23.113 1.00 14.21 6 5200 CALA A 670 1.437 87.798 23.234 1.00 15.38 6 5201 O ALA A 670 1.216 87.26224.323 1.00 15.04 8 5202 CB ALA A 670 3.481 89.251 23.005 1.00 14.71 65203 N THR A 671 1.412 87.143 22.093 1.00 15.66 7 5204 CA THR A 6711.145 85.704 22.056 1.00 15.06 6 5205 C THR A 671 2.463 85.017 21.7371.00 15.13 6 5206 O THR A 671 3.141 85.293 20.734 1.00 16.78 8 5207 CBTHR A 671 0.004 85.374 21.082 1.00 24.32 6 5208 OG1 THR A 671 −1.18186.041 21.584 1.00 19.33 8 5209 CG2 THR A 671 −0.323 83.900 21.063 1.0022.47 6 5210 N THR A 672 2.794 83.967 22.533 1.00 13.36 7 5211 CA THR A672 4.035 83.264 22.249 1.00 14.54 6 5212 C THR A 672 3.911 82.31221.096 1.00 14.80 6 5213 O THR A 672 2.831 81.798 20.772 1.00 13.92 85214 CB THR A 672 4.475 82.464 23.491 1.00 15.06 6 5215 OG1 THR A 6723.485 81.497 23.805 1.00 13.92 8 5216 CG2 THR A 672 4.612 83.376 24.7261.00 15.62 6 5217 N PRO A 673 5.068 81.983 20.499 1.00 16.20 7 5218 CAPRO A 673 5.116 81.063 19.381 1.00 21.02 6 5219 C PRO A 673 4.615 79.69019.691 1.00 17.09 6 5220 O PRO A 673 4.691 79.290 20.893 1.00 16.99 85221 CB PRO A 673 6.606 80.975 18.937 1.00 22.47 6 5222 CG PRO A 6737.309 81.859 19.872 1.00 22.50 6 5223 CD PRO A 673 6.355 82.558 20.8571.00 20.76 6 5224 N THR A 674 4.164 78.885 18.724 1.00 16.36 7 5225 CATHR A 674 3.803 77.518 19.033 1.00 16.04 6 5226 C THR A 674 4.915 76.51618.803 1.00 19.50 6 5227 O THR A 674 4.834 75.399 19.293 1.00 25.45 85228 CB THR A 674 2.613 77.053 18.117 1.00 26.38 6 5229 OG1 THR A 6742.997 77.353 16.786 1.00 31.27 8 5230 CG2 THR A 674 1.409 77.936 18.5211.00 27.63 6 5231 N GLY A 675 5.953 76.981 18.114 1.00 19.68 7 5232 CAGLY A 675 7.035 76.041 17.829 1.00 18.98 6 5233 C GLY A 675 8.164 76.14518.885 1.00 21.20 6 5234 O GLY A 675 7.915 76.654 19.953 1.00 18.10 85235 N ALA A 676 9.349 75.612 18.560 1.00 14.92 7 5236 CA ALA A 67610.419 75.562 19.578 1.00 12.67 6 5237 C ALA A 676 10.845 76.968 19.9741.00 13.87 6 5238 O ALA A 676 11.505 77.096 21.031 1.00 12.93 8 5239 CBALA A 676 11.611 74.771 19.006 1.00 12.85 6 5240 N THR A 677 10.86077.884 19.014 1.00 13.69 7 5241 CA THR A 677 11.444 79.189 19.324 1.0011.81 6 5242 C THR A 677 10.615 80.296 18.686 1.00 13.20 6 5243 O THR A677 9.743 80.066 17.834 1.00 14.64 8 5244 CB THR A 677 12.847 79.36618.681 1.00 14.32 6 5245 OG1 THR A 677 12.712 79.294 17.249 1.00 16.35 85246 CG2 THR A 677 13.851 78.287 19.079 1.00 14.03 6 5247 N GLY A 67810.949 81.490 19.141 1.00 14.25 7 5248 CA GLY A 678 10.413 82.685 18.4371.00 13.38 6 5249 C GLY A 678 10.969 83.958 19.066 1.00 13.68 6 5250 OGLY A 678 11.857 83.956 19.907 1.00 13.62 8 5251 N ASN A 679 10.37485.094 18.654 1.00 13.18 7 5252 CA ASN A 679 10.858 86.398 19.082 1.0011.86 6 5253 C ASN A 679 9.685 87.318 19.466 1.00 14.28 6 5254 O ASN A679 8.718 87.315 18.699 1.00 15.54 8 5255 CB ASN A 679 11.485 87.18017.892 1.00 16.45 6 5256 CG ASN A 679 12.952 86.818 17.758 1.00 25.76 65257 OD1 ASN A 679 13.201 85.708 17.294 1.00 24.19 8 5258 ND2 ASN A 67913.881 87.684 18.146 1.00 26.44 7 5259 N ILE A 680 9.882 88.063 20.5211.00 13.28 7 5260 CA ILE A 680 8.909 89.088 20.948 1.00 14.10 6 5261 CILE A 680 9.758 90.331 21.083 1.00 16.54 6 5262 O ILE A 680 10.67390.366 21.944 1.00 14.10 8 5263 CB ILE A 680 8.224 88.676 22.277 1.0013.96 6 5264 CG1 ILE A 680 7.245 87.519 21.978 1.00 16.92 6 5265 CG2 ILEA 680 7.442 89.919 22.790 1.00 17.42 6 5266 CD1 ILE A 680 6.611 86.86723.218 1.00 15.15 6 5267 N THR A 681 9.363 91.378 20.334 1.00 13.57 75268 CA THR A 681 10.236 92.583 20.392 1.00 12.91 6 5269 C THR A 6819.280 93.751 20.616 1.00 13.01 6 5270 O THR A 681 8.253 93.845 19.9291.00 18.59 8 5271 CB THR A 681 10.904 92.718 18.990 1.00 16.97 6 5272OG1 THR A 681 11.807 91.633 18.765 1.00 17.30 8 5273 CG2 THR A 68111.642 94.052 18.964 1.00 19.53 6 5274 N VAL A 682 9.639 94.595 21.6081.00 15.51 7 5275 CA VAL A 682 8.758 95.732 21.946 1.00 15.78 6 5276 CVAL A 682 9.635 96.952 22.186 1.00 17.87 6 5277 O VAL A 682 10.83896.797 22.256 1.00 15.49 8 5278 CB VAL A 682 7.874 95.472 23.195 1.0016.15 6 5279 CG1 VAL A 682 6.968 94.243 23.002 1.00 16.76 6 5280 CG2 VALA 682 8.730 95.365 24.469 1.00 16.17 6 5281 N THR A 683 9.082 98.16222.306 1.00 15.89 7 5282 CA THR A 683 9.863 99.346 22.623 1.00 15.51 65283 C THR A 683 9.529 99.798 24.046 1.00 16.36 6 5284 O THR A 683 8.37199.703 24.462 1.00 17.59 8 5285 CB THR A 683 9.481 100.473 21.614 1.0022.31 6 5286 OG1 THR A 683 9.916 100.019 20.328 1.00 21.22 8 5287 CG2THR A 683 10.245 101.759 21.921 1.00 19.31 6 5288 N TRP A 684 10.586100.168 24.759 1.00 14.24 7 5289 CA TRP A 684 10.411 100.587 26.154 1.0014.76 6 5290 C TRP A 684 9.369 101.706 26.222 1.00 17.75 6 5291 O TRP A684 9.556 102.695 25.469 1.00 18.74 8 5292 CB TRP A 684 11.745 101.08626.705 1.00 14.95 6 5293 CG TRP A 684 11.696 101.465 28.146 1.00 14.49 65294 CD1 TRP A 684 11.284 102.666 28.672 1.00 15.39 6 5295 CD2 TRP A 68412.163 100.683 29.271 1.00 17.84 6 5296 NE1 TRP A 684 11.376 102.64930.052 1.00 16.11 7 5297 CE2 TRP A 684 11.921 101.440 30.423 1.00 20.666 5298 CE3 TRP A 684 12.764 99.422 29.399 1.00 18.28 6 5299 CZ2 TRP A684 12.245 101.024 31.726 1.00 22.23 6 5300 CZ3 TRP A 684 13.074 98.95930.709 1.00 17.05 6 5301 CH2 TRP A 684 12.791 99.766 31.796 1.00 17.97 65302 N GLN A 685 8.396 101.650 27.102 1.00 17.70 7 5303 CA GLN A 6857.399 102.716 27.315 1.00 18.97 6 5304 C GLN A 685 7.850 103.719 28.3331.00 19.08 6 5305 O GLN A 685 8.067 103.430 29.512 1.00 19.01 8 5306 CBGLN A 685 6.071 102.025 27.745 1.00 15.69 6 5307 CG GLN A 685 5.536101.157 26.596 1.00 17.89 6 5308 CD GLN A 685 4.352 100.283 26.995 1.0018.78 6 5309 OE1 GLN A 685 3.797 99.604 26.110 1.00 20.58 8 5310 NE2 GLNA 685 3.960 100.246 28.267 1.00 17.75 7 5311 N ASN A 686 8.037 105.01127.906 1.00 21.27 7 5312 CA ASN A 686 8.547 106.008 28.836 1.00 20.38 65313 C ASN A 686 7.489 106.854 29.654 1.00 22.87 6 5314 O ASN A 6866.387 106.692 29.016 1.00 22.87 8 5315 CB ASN A 686 9.300 107.060 27.9751.00 24.12 6 5316 CG ASN A 686 10.434 106.404 27.176 1.00 23.38 6 5317OD1 ASN A 686 11.360 105.896 27.821 1.00 22.76 8 5318 ND2 ASN A 68610.376 106.412 25.832 1.00 25.47 7 5319 C11 HEX A 690 38.644 78.01238.228 1.00 27.46 6 5320 O11 HEX A 690 39.147 78.243 39.503 1.00 37.24 85321 C12 HEX A 690 37.596 79.172 38.058 1.00 23.95 6 5322 O12 HEX A 69036.681 78.887 39.109 1.00 20.96 8 5323 C13 HEX A 690 36.915 78.88736.685 1.00 17.64 6 5324 O13 HEX A 690 35.915 79.908 36.442 1.00 18.04 85325 C14 HEX A 690 38.048 79.023 35.670 1.00 17.74 6 5326 C15 HEX A 69039.141 77.967 35.956 1.00 19.52 6 5327 O15 HEX A 690 39.679 78.31237.276 1.00 26.20 8 5328 C16 HEX A 690 40.338 77.919 35.016 1.00 23.71 65329 O16 HEX A 690 40.867 79.240 34.817 1.00 28.38 8 5330 C21 HEX A 69037.609 79.324 33.250 1.00 19.03 6 5331 O21 HEX A 690 37.414 78.56234.414 1.00 18.39 8 5332 C22 HEX A 690 36.237 79.756 32.692 1.00 18.97 65333 O22 HEX A 690 35.419 80.404 33.669 1.00 17.96 8 5334 C23 HEX A 69035.514 78.516 32.153 1.00 16.72 6 5335 O23 HEX A 690 34.355 79.01431.406 1.00 16.31 8 5336 C24 HEX A 690 36.415 77.760 31.174 1.00 12.77 65337 C25 HEX A 690 37.690 77.301 31.955 1.00 17.32 6 5338 O25 HEX A 69038.321 78.596 32.286 1.00 20.72 8 5339 C26 HEX A 690 38.704 76.68130.979 1.00 18.94 6 5340 O26 HEX A 690 39.852 76.182 31.780 1.00 21.07 85341 C31 HEX A 690 35.507 76.403 29.409 1.00 11.28 6 5342 O31 HEX A 69035.723 76.501 30.811 1.00 12.85 8 5343 C32 HEX A 690 34.026 76.11829.118 1.00 13.04 6 5344 O32 HEX A 690 33.259 77.030 29.933 1.00 14.06 85345 C33 HEX A 690 33.654 74.698 29.626 1.00 13.59 6 5346 O33 HEX A 69032.285 74.486 29.158 1.00 12.48 8 5347 C34 HEX A 690 34.578 73.67028.936 1.00 11.83 6 5348 C35 HEX A 690 36.004 74.036 29.487 1.00 14.01 65349 O35 HEX A 690 36.301 75.341 28.930 1.00 12.70 8 5350 C36 HEX A 69037.084 73.167 28.829 1.00 13.71 6 5351 C41 HEX A 690 33.322 71.60128.292 1.00 9.18 6 5352 N41 HEX A 690 34.214 72.300 29.267 1.00 10.73 75353 C42 HEX A 690 33.682 70.074 28.156 1.00 11.48 6 5354 O42 HEX A 69033.732 69.433 29.448 1.00 10.30 8 5355 C43 HEX A 690 35.023 69.96327.455 1.00 10.39 6 5356 O43 HEX A 690 35.686 68.699 27.591 1.00 11.44 85357 C44 HEX A 690 34.791 70.257 25.986 1.00 11.02 6 5358 C45 HEX A 69033.925 71.520 25.899 1.00 10.58 6 5359 C40 HEX A 690 33.262 72.09726.944 1.00 9.08 6 5360 C46 HEX A 690 33.519 71.887 24.466 1.00 12.28 65361 O46 HEX A 690 32.492 71.022 24.020 1.00 12.58 8 5362 C51 HEX A 69036.288 69.864 24.116 1.00 10.88 6 5363 O51 HEX A 690 36.061 70.54125.327 1.00 12.10 8 5364 C52 HEX A 690 37.495 68.906 24.274 1.00 11.69 65365 O52 HEX A 690 37.227 67.917 25.285 1.00 12.57 8 5366 C53 HEX A 69038.717 69.698 24.774 1.00 10.51 6 5367 O53 HEX A 690 39.832 68.75624.609 1.00 11.97 8 5368 C54 HEX A 690 39.025 70.807 23.714 1.00 12.82 65369 C55 HEX A 690 37.748 71.660 23.566 1.00 12.56 6 5370 O55 HEX A 69036.680 70.820 23.133 1.00 11.57 8 5371 C56 HEX A 690 37.890 72.68722.436 1.00 12.61 6 5372 O56 HEX A 690 38.082 72.074 21.134 1.00 19.74 85373 C61 HEX A 690 40.720 72.590 24.188 1.00 22.95 6 5374 O61 HEX A 69039.890 71.572 24.637 1.00 20.26 8 5375 C62 HEX A 690 42.050 72.50024.991 1.00 23.13 6 5376 O62 HEX A 690 42.582 71.189 24.918 1.00 23.06 85377 C63 HEX A 690 41.937 73.006 26.411 1.00 24.03 6 5378 O63 HEX A 69043.280 72.994 26.932 1.00 28.78 8 5379 C64 HEX A 690 41.310 74.40526.428 1.00 25.79 6 5380 O64 HEX A 690 41.035 74.789 27.809 1.00 29.96 85381 C65 HEX A 690 39.918 74.255 25.759 1.00 22.19 6 5382 O65 HEX A 69040.146 73.866 24.404 1.00 22.47 8 5383 C66 HEX A 690 39.177 75.55525.611 1.00 26.12 6 5384 O66 HEX A 690 39.936 76.644 25.149 1.00 24.41 85385 C11 MAL A 691 38.534 71.299 69.464 1.00 19.75 6 5386 O11 MAL A 69138.776 72.581 69.883 1.00 20.21 8 5387 C12 MAL A 691 37.973 71.38468.024 1.00 17.66 6 5388 O12 MAL A 691 38.798 72.262 67.225 1.00 18.71 85389 C13 MAL A 691 36.555 71.949 68.006 1.00 16.03 6 5390 O13 MAL A 69135.969 71.754 66.689 1.00 17.47 8 5391 C14 MAL A 691 35.642 71.10468.925 1.00 15.64 6 5392 C15 MAL A 691 36.269 71.291 70.364 1.00 14.01 65393 O15 MAL A 691 37.561 70.667 70.312 1.00 16.48 8 5394 C16 MAL A 69135.519 70.221 71.238 1.00 19.77 6 5395 O16 MAL A 691 36.004 70.43172.581 1.00 18.54 8 5396 C21 MAL A 691 33.285 70.813 68.523 1.00 18.83 65397 O21 MAL A 691 34.336 71.683 68.968 1.00 17.92 8 5398 C22 MAL A 69132.403 71.638 67.561 1.00 17.24 6 5399 O22 MAL A 691 33.177 72.08366.433 1.00 17.89 8 5400 C23 MAL A 691 31.765 72.820 68.304 1.00 18.41 65401 O23 MAL A 691 30.812 73.419 67.431 1.00 18.30 8 5402 C24 MAL A 69130.951 72.194 69.478 1.00 18.57 6 5403 O24 MAL A 691 30.444 73.29170.263 1.00 19.15 8 5404 C25 MAL A 691 31.923 71.424 70.383 1.00 19.32 65405 O25 MAL A 691 32.521 70.374 69.608 1.00 18.98 8 5406 C26 MAL A 69131.067 70.708 71.468 1.00 15.38 6 5407 O26 MAL A 691 31.944 70.07572.412 1.00 18.74 8 5411 S SUL A 695 11.120 52.018 55.465 1.00 30.54 165412 O1 SUL A 695 11.470 52.936 56.533 1.00 30.07 8 5413 O2 SUL A 69510.034 52.528 54.544 1.00 27.19 8 5414 O3 SUL A 695 12.310 51.631 54.6621.00 34.25 8 5415 O4 SUL A 695 10.566 50.749 56.089 1.00 33.96 8 5451 CAWAT A 692 32.693 60.307 13.017 1.00 11.99 20 5452 CA WAT A 693 26.97579.502 21.970 1.00 10.73 20 5453 CA WAT A 694 37.244 49.841 19.039 1.0013.50 20 5454 OW0 WAT V 1 24.447 79.971 21.858 1.00 9.43 8 5455 OW0 WATV 2 35.686 59.385 24.028 1.00 10.45 8 5456 OW0 WAT V 3 33.934 60.77318.648 1.00 10.63 8 5457 OW0 WAT V 4 35.622 62.751 41.495 1.00 10.88 85458 OW0 WAT V 5 25.780 77.914 20.486 1.00 10.75 8 5459 OW0 WAT V 621.776 77.285 28.879 1.00 10.81 8 5460 OW0 WAT V 7 29.415 69.145 19.4001.00 10.86 8 5461 OW0 WAT V 8 29.138 80.312 22.631 1.00 10.86 8 5462 OW0WAT V 9 27.613 72.037 24.448 1.00 10.77 8 5463 OW0 WAT V 10 31.16477.784 19.615 1.00 10.85 8 5464 OW0 WAT V 11 32.790 66.917 36.378 1.0010.94 8 5465 OW0 WAT V 12 34.127 70.240 32.929 1.00 11.18 8 5466 OW0 WATV 13 33.080 60.581 23.767 1.00 11.11 8 5467 OW0 WAT V 14 37.235 54.60119.600 1.00 11.38 8 5468 OW0 WAT V 15 26.119 65.542 21.574 1.00 11.07 85469 OW0 WAT V 16 28.484 64.486 20.522 1.00 11.49 8 5470 OW0 WAT V 1728.194 73.536 36.853 1.00 11.53 8 5471 OW0 WAT V 18 16.618 66.275 36.8061.00 11.68 8 5472 OW0 WAT V 19 26.088 62.658 22.854 1.00 11.54 8 5473OW0 WAT V 20 37.981 63.919 14.127 1.00 11.77 8 5474 OW0 WAT V 21 34.93260.656 13.769 1.00 11.70 8 5475 OW0 WAT V 22 41.499 60.656 38.722 1.0011.54 8 5476 OW0 WAT V 23 40.945 66.711 20.205 1.00 11.65 8 5477 OW0 WATV 24 8.905 64.107 34.370 1.00 11.68 8 5478 OW0 WAT V 25 19.426 72.35640.893 1.00 11.74 8 5479 OW0 WAT V 26 20.321 82.331 35.376 1.00 11.77 85480 OW0 WAT V 27 14.993 64.250 37.502 1.00 11.91 8 5481 OW0 WAT V 2831.504 68.673 10.842 1.00 12.08 8 5482 OW0 WAT V 29 37.606 61.402 40.1671.00 11.91 8 5483 OW0 WAT V 30 16.372 70.863 38.933 1.00 11.99 8 5484OW0 WAT V 31 7.950 69.079 31.258 1.00 12.08 8 5485 OW0 WAT V 32 19.52873.999 43.164 1.00 12.10 8 5486 OW0 WAT V 33 16.210 66.954 39.606 1.0012.02 8 5487 OW0 WAT V 34 32.679 63.267 29.330 1.00 12.26 8 5488 OW0 WATV 35 13.649 74.479 39.683 1.00 12.21 8 5489 OW0 WAT V 36 16.357 79.63122.013 1.00 12.26 8 5490 OW0 WAT V 37 21.471 63.888 43.225 1.00 12.25 85491 OW0 WAT V 38 42.464 66.587 23.881 1.00 12.49 8 5492 OW0 WAT V 3931.355 60.893 19.838 1.00 12.31 8 5493 OW0 WAT V 40 16.930 64.546 40.9811.00 12.36 8 5494 OW0 WAT V 41 10.918 81.011 32.425 1.00 12.42 8 5495OW0 WAT V 42 8.358 78.559 35.685 1.00 12.49 8 5496 OW0 WAT V 43 22.05271.621 41.190 1.00 12.24 8 5497 OW0 WAT V 44 8.226 66.640 35.276 1.0012.62 8 5498 OW0 WAT V 45 6.031 77.562 36.868 1.00 12.35 8 5499 OW0 WATV 46 43.919 60.734 40.175 1.00 12.51 8 5500 OW0 WAT V 48 11.578 73.47841.191 1.00 12.62 8 5501 OW0 WAT V 49 35.256 52.308 26.203 1.00 12.50 85502 OW0 WAT V 50 22.628 81.739 22.782 1.00 12.52 8 5503 OW0 WAT V 5141.171 68.357 22.292 1.00 12.78 8 5504 OW0 WAT V 52 34.554 71.110 10.7831.00 12.58 8 5505 OW0 WAT V 53 39.554 70.543 28.407 1.00 12.73 8 5506OW0 WAT V 54 14.970 66.671 43.779 1.00 12.94 8 5507 OW0 WAT V 55 14.79281.581 20.763 1.00 12.92 8 5508 OW0 WAT V 56 30.205 75.643 31.109 1.0012.90 8 5509 OW0 WAT V 57 16.697 82.536 30.534 1.00 13.09 8 5510 OW0 WATV 58 38.776 53.289 57.732 1.00 13.10 8 5511 OW0 WAT V 59 31.565 49.27320.064 1.00 13.22 8 5512 OW0 WAT V 60 20.200 85.147 36.037 1.00 13.29 85513 OW0 WAT V 61 25.657 54.513 45.949 1.00 13.32 8 5514 OW0 WAT V 6237.048 52.273 18.284 1.00 13.46 8 5515 OW0 WAT V 63 30.032 67.305 53.9381.00 13.27 8 5516 OW0 WAT V 64 32.331 68.357 33.829 1.00 13.58 8 5517OW0 WAT V 65 23.329 85.511 30.252 1.00 13.33 8 5518 OW0 WAT V 66 20.24661.387 18.981 1.00 13.61 8 5519 OW0 WAT V 67 28.775 74.856 40.336 1.0013.65 8 5520 OW0 WAT V 68 32.567 68.924 43.607 1.00 13.35 8 5521 OW0 WATV 69 10.838 68.713 42.880 1.00 13.33 8 5522 OW0 WAT V 70 12.859 61.51843.606 1.00 13.90 8 5523 OW0 WAT V 71 45.207 60.214 32.334 1.00 13.77 85524 OW0 WAT V 72 27.427 66.987 53.108 1.00 13.75 8 5525 OW0 WAT V 7319.074 63.276 42.264 1.00 13.66 8 5526 OW0 WAT V 74 36.934 75.592 8.2701.00 13.53 8 5527 OW0 WAT V 75 27.574 81.410 6.013 1.00 14.19 8 5528 OW0WAT V 76 30.621 83.670 31.215 1.00 14.28 8 5529 OW0 WAT V 77 42.51470.356 20.822 1.00 14.45 8 5530 OW0 WAT V 78 12.529 75.168 22.815 1.0014.52 8 5531 OW0 WAT V 79 39.891 56.461 11.992 1.00 14.18 8 5532 OW0 WATV 80 30.677 68.114 68.620 1.00 14.47 8 5533 OW0 WAT V 81 33.218 64.22436.711 1.00 14.46 8 5534 OW0 WAT V 82 12.035 74.811 37.533 1.00 14.63 85535 OW0 WAT V 83 15.981 73.538 38.669 1.00 14.16 8 5536 OW0 WAT V 8410.686 81.113 35.947 1.00 14.90 8 5537 OW0 WAT V 85 25.562 71.871 51.2871.00 14.81 8 5538 OW0 WAT V 86 29.447 83.564 16.644 1.00 14.86 8 5539OW0 WAT V 87 13.480 81.300 31.112 1.00 14.85 8 5540 OW0 WAT V 88 5.77480.076 41.775 1.00 14.92 8 5541 OW0 WAT V 89 47.914 63.828 68.644 1.0014.87 8 5542 OW0 WAT V 90 34.743 77.662 45.101 1.00 15.02 8 5543 OW0 WATV 91 24.427 76.387 7.359 1.00 15.03 8 5544 OW0 WAT V 92 −2.703 63.47138.845 1.00 15.46 8 5545 OW0 WAT V 93 14.681 69.092 37.625 1.00 15.14 85546 OW0 WAT V 94 28.123 74.474 42.954 1.00 15.12 8 5547 OW0 WAT V 9523.589 80.407 29.737 1.00 15.19 8 5548 OW0 WAT V 96 28.941 64.658 47.2811.00 15.32 8 5549 OW0 WAT V 97 33.848 82.923 7.441 1.00 15.09 8 5550 OW0WAT V 98 50.687 59.709 65.034 1.00 15.32 8 5551 OW0 WAT V 99 29.97780.264 14.804 1.00 15.36 8 5552 OW0 WAT V 100 25.916 52.607 44.011 1.0015.58 8 5553 OW0 WAT V 101 6.765 62.176 32.083 1.00 15.56 8 5554 OW0 WATV 102 13.107 89.810 20.076 1.00 15.94 8 5555 OW0 WAT V 103 11.601 78.29236.745 1.00 15.75 8 5556 OW0 WAT V 104 14.144 58.009 41.510 1.00 15.84 85557 OW0 WAT V 105 44.010 71.623 35.990 1.00 15.89 8 5558 OW0 WAT V 10621.168 82.474 32.738 1.00 16.12 8 5559 OW0 WAT V 107 28.667 48.68846.155 1.00 16.35 8 5560 OW0 WAT V 108 25.610 86.818 38.209 1.00 16.18 85561 OW0 WAT V 109 29.070 89.992 31.492 1.00 16.47 8 5562 OW0 WAT V 1101.291 75.000 41.091 1.00 16.32 8 5563 OW0 WAT V 111 34.624 56.600 71.3281.00 16.34 8 5564 OW0 WAT V 112 28.281 69.481 68.152 1.00 16.52 8 5565OW0 WAT V 113 26.135 87.038 35.304 1.00 16.58 8 5566 OW0 WAT V 11435.168 78.123 51.153 1.00 16.64 8 5567 OW0 WAT V 115 19.827 81.28146.203 1.00 16.48 8 5568 OW0 WAT V 116 30.082 84.087 8.323 1.00 16.75 85569 OW0 WAT V 117 45.164 71.238 15.992 1.00 16.58 8 5570 OW0 WAT V 118−2.555 86.829 29.585 1.00 16.73 8 5571 OW0 WAT V 119 1.879 75.860 26.2971.00 16.96 8 5572 OW0 WAT V 120 20.960 94.415 22.713 1.00 16.87 8 5573OW0 WAT V 121 12.300 72.626 21.951 1.00 16.94 8 5574 OW0 WAT V 12221.720 86.954 37.648 1.00 17.08 8 5575 OW0 WAT V 123 17.342 46.05229.967 1.00 16.89 8 5576 OW0 WAT V 124 15.847 84.337 34.562 1.00 16.74 85577 OW0 WAT V 125 −3.241 60.294 45.682 1.00 16.67 8 5578 OW0 WAT V 12611.587 104.148 24.323 1.00 17.24 8 5579 OW0 WAT V 127 28.501 56.85251.441 1.00 17.40 8 5580 OW0 WAT V 128 14.206 82.937 18.392 1.00 17.21 85581 OW0 WAT V 129 41.516 56.407 63.525 1.00 17.22 8 5582 OW0 WAT V 13036.936 73.986 40.016 1.00 17.65 8 5583 OW0 WAT V 131 20.790 40.11527.752 1.00 17.53 8 5584 OW0 WAT V 132 45.240 52.146 20.212 1.00 17.55 85585 OW0 WAT V 133 41.799 49.726 28.892 1.00 17.29 8 5586 OW0 WAT V 13423.108 66.755 60.083 1.00 17.41 8 5587 OW0 WAT V 135 26.863 48.80541.435 1.00 17.67 8 5588 OW0 WAT V 136 27.488 90.699 28.339 1.00 17.76 85589 OW0 WAT V 137 0.191 69.111 49.096 1.00 17.78 8 5590 OW0 WAT V 13834.447 43.232 33.946 1.00 17.85 8 5591 OW0 WAT V 139 22.589 64.04449.415 1.00 18.18 8 5592 OW0 WAT V 140 17.697 81.339 35.462 1.00 17.98 85593 OW0 WAT V 141 2.444 96.838 37.934 1.00 18.09 8 5594 OW0 WAT V 14235.347 81.251 39.545 1.00 17.94 8 5595 OW0 WAT V 143 14.511 56.29749.652 1.00 18.35 8 5596 OW0 WAT V 144 10.014 71.654 20.618 1.00 18.11 85597 OW0 WAT V 145 47.629 63.815 18.991 1.00 18.25 8 5598 OW0 WAT V 14615.832 79.962 31.635 1.00 18.52 8 5599 OW0 WAT V 147 35.482 76.42839.594 1.00 18.64 8 5600 OW0 WAT V 149 16.532 67.334 48.159 1.00 18.61 85601 OW0 WAT V 150 32.280 83.173 33.550 1.00 18.44 8 5602 OW0 WAT V 15135.037 62.885 71.628 1.00 18.62 8 5603 OW0 WAT V 152 14.756 56.44828.743 1.00 18.87 8 5604 OW0 WAT V 153 51.007 64.138 32.515 1.00 18.45 85605 OW0 WAT V 154 44.683 55.406 52.749 1.00 18.86 8 5606 OW0 WAT V 15530.803 47.286 18.413 1.00 19.00 8 5607 OW0 WAT V 156 21.419 87.00831.586 1.00 18.86 8 5608 OW0 WAT V 157 27.471 54.562 13.822 1.00 18.93 85609 OW0 WAT V 158 19.938 85.031 32.888 1.00 18.77 8 5610 OW0 WAT V 16023.159 58.927 72.012 1.00 19.01 8 5611 OW0 WAT V 161 20.470 84.77318.243 1.00 19.09 8 5612 OW0 WAT V 162 15.077 66.831 13.792 1.00 18.88 85613 OW0 WAT V 164 34.016 76.548 58.886 1.00 19.18 8 5614 OW0 WAT V 1651.791 96.077 35.490 1.00 19.39 8 5615 OW0 WAT V 168 16.921 65.681 50.1731.00 19.74 8 5616 OW0 WAT V 169 36.015 49.508 63.823 1.00 19.75 8 5617OW0 WAT V 170 19.146 93.639 20.716 1.00 19.72 8 5618 OW0 WAT V 17141.081 74.262 43.114 1.00 19.99 8 5619 OW0 WAT V 172 27.356 86.83441.150 1.00 19.86 8 5620 OW0 WAT V 173 32.541 61.241 6.239 1.00 19.49 85621 OW0 WAT V 174 51.971 65.011 17.317 1.00 20.07 8 5622 OW0 WAT V 17536.754 79.161 49.332 1.00 19.96 8 5623 OW0 WAT V 176 21.529 68.51652.600 1.00 19.88 8 5624 OW0 WAT V 177 52.175 64.476 48.627 1.00 19.48 85625 OW0 WAT V 178 47.687 55.894 28.556 1.00 19.85 8 5626 OW0 WAT V 18028.309 57.733 12.302 1.00 19.86 8 5627 OW0 WAT V 181 19.852 88.58539.017 1.00 20.03 8 5628 OW0 WAT V 182 48.116 65.053 11.253 1.00 19.75 85629 OW0 WAT V 183 45.728 49.401 46.755 1.00 20.07 8 5630 OW0 WAT V 18423.090 51.403 56.173 1.00 19.76 8 5631 OW0 WAT V 185 23.972 69.60453.226 1.00 20.10 8 5632 OW0 WAT V 186 49.679 65.500 55.245 1.00 19.98 85633 OW0 WAT V 187 50.720 57.388 48.688 1.00 20.39 8 5634 OW0 WAT V 18834.857 63.152 38.228 1.00 20.23 8 5635 OW0 WAT V 189 37.511 43.02919.233 1.00 20.32 8 5636 OW0 WAT V 190 50.567 67.974 10.449 1.00 20.64 85637 OW0 WAT V 191 29.875 92.014 24.922 1.00 20.34 8 5638 OW0 WAT V 1924.055 100.811 36.567 1.00 20.35 8 5639 OW0 WAT V 194 23.592 87.85932.780 1.00 20.02 8 5640 OW0 WAT V 195 43.898 69.204 9.296 1.00 20.35 85641 OW0 WAT V 196 17.503 91.553 19.944 1.00 20.36 8 5642 OW0 WAT V 19722.079 71.014 56.203 1.00 20.50 8 5643 OW0 WAT V 198 24.611 90.27832.659 1.00 20.71 8 5644 OW0 WAT V 199 15.822 79.667 34.285 1.00 20.71 85645 OW0 WAT V 200 41.507 64.519 35.769 1.00 20.47 8 5646 OW0 WAT V 20150.582 63.510 21.444 1.00 20.44 8 5647 OW0 WAT V 202 −4.254 88.78128.481 1.00 20.69 8 5648 OW0 WAT V 203 41.289 48.120 25.349 1.00 20.50 85649 OW0 WAT V 204 33.838 47.522 55.491 1.00 20.42 8 5650 OW0 WAT V 20528.696 42.611 30.481 1.00 21.10 8 5651 OW0 WAT V 206 29.680 89.47934.207 1.00 20.71 8 5652 OW0 WAT V 207 13.375 82.989 38.528 1.00 20.79 85653 OW0 WAT V 208 −0.381 94.652 35.925 1.00 20.71 8 5654 OW0 WAT V 20932.894 53.249 7.401 1.00 20.79 8 5655 OW0 WAT V 210 47.202 71.009 63.9611.00 20.83 8 5656 OW0 WAT V 211 16.432 73.589 49.935 1.00 20.64 8 5657OW0 WAT V 212 36.761 42.123 23.718 1.00 20.49 8 5658 OW0 WAT V 213 1.32698.176 25.977 1.00 21.14 8 5659 OW0 WAT V 215 32.369 84.143 13.694 1.0021.27 8 5660 OW0 WAT V 216 1.000 72.006 27.168 1.00 21.23 8 5661 OW0 WATV 217 21.907 50.669 62.000 1.00 21.19 8 5662 OW0 WAT V 218 30.956 41.73821.314 1.00 21.03 8 5663 OW0 WAT V 219 36.121 71.463 4.684 1.00 21.46 85664 OW0 WAT V 220 13.404 81.016 34.970 1.00 21.65 8 5665 OW0 WAT V 22122.957 65.844 62.604 1.00 21.35 8 5666 OW0 WAT V 222 4.260 99.337 39.6491.00 21.63 8 5667 OW0 WAT V 223 17.535 84.263 32.555 1.00 20.98 8 5668OW0 WAT V 224 16.496 59.065 45.746 1.00 21.66 8 5669 OW0 WAT V 22516.576 52.574 34.164 1.00 21.65 8 5670 OW0 WAT V 226 30.825 51.40613.432 1.00 21.28 8 5671 OW0 WAT V 227 39.177 82.848 23.121 1.00 21.63 85672 OW0 WAT V 229 19.108 58.790 36.143 1.00 21.40 8 5673 OW0 WAT V 23019.087 75.378 50.063 1.00 21.22 8 5674 OW0 WAT V 231 47.413 69.88116.583 1.00 21.29 8 5675 OW0 WAT V 232 26.686 91.040 31.058 1.00 21.61 85676 OW0 WAT V 233 29.036 52.089 61.852 1.00 21.25 8 5677 OW0 WAT V 23436.187 79.293 46.671 1.00 21.45 8 5678 OW0 WAT V 235 37.289 74.83565.582 1.00 21.65 8 5679 OW0 WAT V 236 −0.428 68.770 30.109 1.00 21.94 85680 OW0 WAT V 237 50.762 57.829 44.061 1.00 22.15 8 5681 OW0 WAT V 23845.167 70.565 24.893 1.00 22.00 8 5682 OW0 WAT V 239 28.609 48.60951.930 1.00 22.03 8 5683 OW0 WAT V 241 2.366 94.552 38.603 1.00 21.97 85684 OW0 WAT V 242 9.365 68.970 20.742 1.00 22.04 8 5685 OW0 WAT V 24338.583 85.642 29.447 1.00 21.90 8 5686 OW0 WAT V 244 24.639 49.54255.081 1.00 22.42 8 5687 OW0 WAT V 245 18.177 95.474 18.838 1.00 22.69 85688 OW0 WAT V 246 37.307 43.276 33.862 1.00 22.90 8 5689 OW0 WAT V 24723.478 86.290 16.425 1.00 21.85 8 5690 OW0 WAT V 248 43.569 60.46672.156 1.00 23.10 8 5691 OW0 WAT V 249 23.281 40.658 26.691 1.00 22.77 85692 OW0 WAT V 250 8.761 65.837 24.376 1.00 23.00 8 5693 OW0 WAT V 25127.215 72.803 60.509 1.00 22.60 8 5694 OW0 WAT V 252 16.174 91.01444.772 1.00 22.53 8 5695 OW0 WAT V 253 3.297 98.395 35.969 1.00 23.15 85696 OW0 WAT V 254 10.918 68.974 53.447 1.00 23.22 8 5697 OW0 WAT V 255−5.802 66.167 37.375 1.00 23.15 8 5698 OW0 WAT V 256 8.490 91.603 44.0991.00 22.65 8 5699 OW0 WAT V 257 9.234 73.507 16.552 1.00 22.92 8 5700OW0 WAT V 258 15.730 56.257 16.556 1.00 23.08 8 5701 OW0 WAT V 25919.989 82.268 13.713 1.00 22.90 8 5702 OW0 WAT V 260 27.613 49.79260.562 1.00 23.09 8 5703 OW0 WAT V 261 26.408 61.061 10.006 1.00 23.11 85704 OW0 WAT V 262 14.277 70.834 12.781 1.00 23.32 8 5705 OW0 WAT V 263−3.969 72.948 34.601 1.00 22.98 8 5706 OW0 WAT V 264 −1.028 93.82938.475 1.00 23.17 8 5707 OW0 WAT V 265 19.230 101.476 27.805 1.00 22.958 5708 OW0 WAT V 266 17.914 54.281 55.523 1.00 23.31 8 5709 OW0 WAT V267 −1.163 64.024 50.895 1.00 23.41 8 5710 OW0 WAT V 268 16.209 48.60729.481 1.00 23.45 8 5711 OW0 WAT V 269 35.070 63.595 75.008 1.00 23.90 85712 OW0 WAT V 270 38.343 43.626 21.918 1.00 23.33 8 5713 OW0 WAT V 27132.197 85.153 37.181 1.00 23.49 8 5714 OW0 WAT V 272 28.789 71.41966.331 1.00 22.79 8 5715 OW0 WAT V 273 41.806 79.697 18.591 1.00 23.39 85716 OW0 WAT V 274 38.127 43.105 36.443 1.00 23.39 8 5717 OW0 WAT V 27516.104 65.021 59.364 1.00 23.44 8 5718 OW0 WAT V 276 −6.314 69.71039.367 1.00 24.17 8 5719 OW0 WAT V 277 25.476 86.458 13.742 1.00 23.04 85720 OW0 WAT V 278 0.680 86.883 37.755 1.00 23.27 8 5721 OW0 WAT V 27933.015 81.157 29.976 1.00 23.30 8 5722 OW0 WAT V 280 1.763 88.744 19.5241.00 23.68 8 5723 OW0 WAT V 281 13.574 55.293 46.773 1.00 23.63 8 5724OW0 WAT V 282 13.480 62.142 18.325 1.00 23.48 8 5725 OW0 WAT V 28319.332 56.925 43.429 1.00 23.84 8 5726 OW0 WAT V 284 7.117 53.127 42.9021.00 23.57 8 5727 OW0 WAT V 285 27.829 78.220 46.852 1.00 24.20 8 5728OW0 WAT V 286 49.295 57.105 51.124 1.00 23.77 8 5729 OW0 WAT V 28713.680 105.356 27.022 1.00 24.03 8 5730 OW0 WAT V 288 17.824 106.63932.939 1.00 24.44 8 5731 OW0 WAT V 289 15.542 66.715 53.507 1.00 24.42 85732 OW0 WAT V 290 27.050 47.324 23.573 1.00 24.19 8 5733 OW0 WAT V 29139.482 73.577 31.816 1.00 24.19 8 5734 OW0 WAT V 292 10.356 77.63816.052 1.00 23.96 8 5735 OW0 WAT V 293 24.405 50.730 63.252 1.00 24.31 85736 OW0 WAT V 294 15.639 54.776 31.091 1.00 24.31 8 5737 OW0 WAT V 295−5.196 74.449 41.013 1.00 24.22 8 5738 OW0 WAT V 296 40.985 72.33529.872 1.00 24.55 8 5739 OW0 WAT V 297 48.449 77.051 18.858 1.00 24.18 85740 OW0 WAT V 298 25.992 92.521 26.784 1.00 24.84 8 5741 OW0 WAT V 29945.814 49.306 39.112 1.00 24.65 8 5742 OW0 WAT V 300 44.725 55.96811.440 1.00 24.94 8 5743 OW0 WAT V 301 20.058 84.809 46.357 1.00 24.73 85744 OW0 WAT V 302 18.079 50.984 17.334 1.00 24.58 8 5745 OW0 WAT V 30317.020 65.666 56.879 1.00 24.81 8 5746 OW0 WAT V 304 44.682 72.66122.319 1.00 24.66 8 5747 OW0 WAT V 305 0.091 75.457 45.401 1.00 24.37 85748 OW0 WAT V 306 50.222 58.393 53.380 1.00 24.90 8 5749 OW0 WAT V 30744.639 52.674 53.486 1.00 25.29 8 5750 OW0 WAT V 308 49.725 64.82752.493 1.00 24.60 8 5751 OW0 WAT V 309 39.542 61.118 7.698 1.00 24.82 85752 OW0 WAT V 310 41.190 79.148 23.073 1.00 25.15 8 5753 OW0 WAT V 3111.598 80.899 39.623 1.00 24.95 8 5754 OW0 WAT V 312 25.053 45.139 19.8171.00 24.92 8 5755 OW0 WAT V 313 16.135 84.191 47.663 1.00 25.20 8 5756OW0 WAT V 314 11.381 71.857 49.110 1.00 25.29 8 5757 OW0 WAT V 315−4.512 57.278 42.326 1.00 25.43 8 5758 OW0 WAT V 316 3.805 93.061 22.7901.00 25.09 8 5759 OW0 WAT V 317 34.832 82.782 37.221 1.00 25.16 8 5760OW0 WAT V 318 3.711 95.706 23.179 1.00 25.31 8 5761 OW0 WAT V 319 20.20970.499 54.469 1.00 25.69 8 5762 OW0 WAT V 320 11.697 68.339 56.789 1.0025.01 8 5763 OW0 WAT V 321 7.254 91.019 18.448 1.00 25.40 8 5764 OW0 WATV 322 42.661 49.979 21.111 1.00 25.81 8 5765 OW0 WAT V 323 17.078 70.89250.293 1.00 25.51 8 5766 OW0 WAT V 324 49.200 60.915 31.600 1.00 25.53 85767 OW0 WAT V 325 31.661 71.214 4.552 1.00 25.64 8 5768 OW0 WAT V 326−2.062 96.310 27.990 1.00 25.87 8 5769 OW0 WAT V 327 39.125 80.23056.164 1.00 26.25 8 5770 OW0 WAT V 328 48.433 70.294 57.525 1.00 25.87 85771 OW0 WAT V 329 −2.772 64.990 34.941 1.00 25.71 8 5772 OW0 WAT V 33035.352 40.001 22.353 1.00 25.96 8 5773 OW0 WAT V 331 34.557 81.62746.792 1.00 26.23 8 5774 OW0 WAT V 332 23.250 92.581 31.676 1.00 26.20 85775 OW0 WAT V 333 23.167 53.251 13.715 1.00 25.74 8 5776 OW0 WAT V 33420.707 52.356 39.202 1.00 25.65 8 5777 OW0 WAT V 335 4.870 93.727 41.2641.00 26.54 8 5778 OW0 WAT V 336 0.053 71.401 29.885 1.00 25.67 8 5779OW0 WAT V 337 20.015 56.517 72.324 1.00 25.86 8 5780 OW0 WAT V 33813.826 74.132 49.507 1.00 26.36 8 5781 OW0 WAT V 339 44.958 71.63228.685 1.00 26.80 8 5782 OW0 WAT V 340 −0.093 73.784 33.119 1.00 26.07 85783 OW0 WAT V 341 49.630 56.579 40.106 1.00 26.64 8 5784 OW0 WAT V 34215.628 79.186 45.524 1.00 26.42 8 5785 OW0 WAT V 343 31.176 91.86730.769 1.00 26.10 8 5786 OW0 WAT V 344 15.626 67.643 55.543 1.00 26.46 85787 OW0 WAT V 345 21.398 95.678 38.839 1.00 26.79 8 5788 OW0 WAT V 34641.099 41.982 39.915 1.00 26.66 8 5789 OW0 WAT V 347 22.442 79.888 2.6611.00 26.18 8 5790 OW0 WAT V 348 44.448 72.532 39.099 1.00 27.08 8 5791OW0 WAT V 349 40.265 82.719 10.175 1.00 26.27 8 5792 OW0 WAT V 35040.934 43.657 30.662 1.00 27.04 8 5793 OW0 WAT V 351 −1.666 97.21332.163 1.00 27.31 8 5794 OW0 WAT V 352 −8.111 67.221 45.293 1.00 27.12 85795 OW0 WAT V 353 16.355 56.614 42.471 1.00 27.10 8 5796 OW0 WAT V 35411.346 65.531 19.934 1.00 27.40 8 5797 OW0 WAT V 355 11.189 105.27521.949 1.00 27.29 8 5798 OW0 WAT V 356 23.545 83.502 8.615 1.00 27.06 85799 OW0 WAT V 357 22.122 49.913 14.384 1.00 27.06 8 5800 OW0 WAT V 3586.833 52.668 34.000 1.00 27.79 8 5801 OW0 WAT V 359 30.479 47.598 56.6661.00 27.66 8 5802 OW0 WAT V 360 33.166 42.826 19.802 1.00 27.33 8 5803OW0 WAT V 361 24.029 55.851 13.947 1.00 28.08 8 5804 OW0 WAT V 36239.488 85.709 20.632 1.00 27.01 8 5805 OW0 WAT V 363 2.130 49.916 43.0491.00 27.26 8 5806 OW0 WAT V 364 35.616 41.373 27.626 1.00 27.13 8 5807OW0 WAT V 365 50.664 58.560 41.450 1.00 26.59 8 5808 OW0 WAT V 36630.943 49.068 15.778 1.00 26.98 8 5809 OW0 WAT V 367 43.193 44.16634.878 1.00 26.97 8 5810 OW0 WAT V 368 6.994 74.430 21.876 1.00 27.26 85811 OW0 WAT V 369 34.427 88.111 38.939 1.00 27.30 8 5812 OW0 WAT V 3701.636 93.582 40.791 1.00 27.54 8 5813 OW0 WAT V 371 5.971 98.241 21.5041.00 27.42 8 5814 OW0 WAT V 372 29.223 75.038 60.445 1.00 26.93 8 5815OW0 WAT V 373 31.316 53.650 9.481 1.00 27.85 8 5816 OW0 WAT V 374 43.93956.548 55.050 1.00 27.63 8 5817 OW0 WAT V 375 46.559 74.427 54.610 1.0027.46 8 5818 OW0 WAT V 376 26.961 70.400 70.205 1.00 28.10 8 5819 OW0WAT V 377 48.989 57.080 35.445 1.00 28.37 8 5820 OW0 WAT V 378 14.95047.050 27.899 1.00 27.90 8 5821 OW0 WAT V 379 46.760 46.713 39.616 1.0027.67 8 5822 OW0 WAT V 380 −1.380 79.896 38.771 1.00 28.02 8 5823 OW0WAT V 381 12.690 81.625 15.826 1.00 28.03 8 5824 OW0 WAT V 382 10.617104.039 32.646 1.00 28.19 8 5825 OW0 WAT V 383 13.859 80.594 13.625 1.0027.99 8 5826 OW0 WAT V 384 7.322 72.231 20.822 1.00 28.35 8 5827 OW0 WATV 385 29.284 46.632 44.658 1.00 28.26 8 5828 OW0 WAT V 386 18.064 50.55924.862 1.00 28.35 8 5829 OW0 WAT V 387 35.054 45.412 46.835 1.00 28.58 85830 OW0 WAT V 388 22.478 83.558 13.277 1.00 28.32 8 5831 OW0 WAT V 38910.928 67.510 14.236 1.00 28.65 8 5832 OW0 WAT V 390 33.397 82.24649.220 1.00 27.37 8 5833 OW0 WAT V 391 23.434 88.556 18.508 1.00 28.95 85834 OW0 WAT V 392 29.832 42.212 39.251 1.00 28.21 8 5835 OW0 WAT V 39315.076 70.102 51.758 1.00 27.91 8 5836 OW0 WAT V 394 35.566 48.45366.263 1.00 28.16 8 5837 OW0 WAT V 395 34.691 46.594 49.301 1.00 28.85 85838 OW0 WAT V 396 39.702 74.440 36.238 1.00 28.77 8 5839 OW0 WAT V 39750.176 56.086 14.851 1.00 28.75 8 5840 OW0 WAT V 398 14.115 57.83459.211 1.00 27.83 8 5841 OW0 WAT V 399 38.189 49.702 11.383 1.00 29.29 85842 OW0 WAT V 400 3.241 100.941 39.033 1.00 28.47 8 5843 OW0 WAT V 40144.298 73.510 63.099 1.00 28.91 8 5844 OW0 WAT V 402 7.061 75.135 47.5441.00 28.59 8 5845 OW0 WAT V 403 5.477 86.910 42.452 1.00 29.56 8 5846OW0 WAT V 404 25.564 72.515 56.246 1.00 29.09 8 5847 OW0 WAT V 40525.075 41.160 32.189 1.00 29.20 8 5848 OW0 WAT V 406 2.074 56.387 58.8541.00 28.86 8 5849 OW0 WAT V 407 47.163 58.038 33.355 1.00 28.76 8 5850OW0 WAT V 408 27.438 44.407 21.116 1.00 28.21 8 5851 OW0 WAT V 40932.690 89.765 34.445 1.00 29.13 8 5852 OW0 WAT V 410 8.726 56.984 33.8751.00 28.81 8 5853 OW0 WAT V 411 −2.765 74.847 45.763 1.00 28.58 8 5854OW0 WAT V 412 9.880 76.028 48.593 1.00 29.43 8 5855 OW0 WAT V 413 18.58755.405 41.191 1.00 28.66 8 5856 OW0 WAT V 414 0.831 95.595 23.928 1.0028.90 8 5857 OW0 WAT V 415 18.167 58.042 65.360 1.00 28.57 8 5858 OW0WAT V 416 42.814 47.661 27.620 1.00 29.34 8 5859 OW0 WAT V 417 19.22689.316 19.020 1.00 29.13 8 5860 OW0 WAT V 418 17.933 82.283 11.952 1.0028.48 8 5861 OW0 WAT V 419 44.723 79.313 13.493 1.00 30.12 8 5862 OW0WAT V 420 34.399 78.316 0.819 1.00 29.81 8 5863 OW0 WAT V 421 28.28272.460 57.888 1.00 29.12 8 5864 OW0 WAT V 422 50.448 63.547 18.793 1.0029.31 8 5865 OW0 WAT V 423 43.033 55.323 65.913 1.00 29.32 8 5866 OW0WAT V 424 45.865 51.168 51.498 1.00 29.29 8 5867 OW0 WAT V 425 12.84459.751 19.386 1.00 29.45 8 5868 OW0 WAT V 426 −3.707 82.697 22.959 1.0029.58 8 5869 OW0 WAT V 427 28.989 45.171 18.941 1.00 29.97 8 5870 OW0WAT V 428 14.689 65.149 11.472 1.00 29.76 8 5871 OW0 WAT V 429 49.96274.061 53.225 1.00 29.59 8 5872 OW0 WAT V 430 26.674 46.428 17.647 1.0029.59 8 5873 OW0 WAT V 431 32.017 64.281 73.846 1.00 29.67 8 5874 OW0WAT V 432 −1.685 89.735 36.396 1.00 29.42 8 5875 OW0 WAT V 433 35.32690.671 32.858 1.00 30.08 8 5876 OW0 WAT V 434 −5.217 86.519 22.737 1.0030.64 8 5877 OW0 WAT V 435 22.655 40.619 31.468 1.00 30.18 8 5878 OW0WAT V 436 9.970 66.686 21.940 1.00 30.16 8 5879 OW0 WAT V 437 22.156103.267 41.579 1.00 28.97 8 5880 OW0 WAT V 438 40.919 45.553 23.996 1.0030.13 8 5881 OW0 WAT V 439 24.378 42.994 18.498 1.00 30.29 8 5882 OW0WAT V 440 27.456 90.485 38.760 1.00 29.87 8 5883 OW0 WAT V 441 41.62878.372 57.406 1.00 30.24 8 5884 OW0 WAT V 442 10.162 67.365 58.879 1.0030.51 8 5885 OW0 WAT V 443 7.899 70.258 55.642 1.00 29.98 8 5886 OW0 WATV 444 7.439 62.721 58.664 1.00 30.04 8 5887 OW0 WAT V 445 30.182 60.2965.170 1.00 30.62 8 5888 OW0 WAT V 446 36.835 87.065 16.010 1.00 30.22 85889 OW0 WAT V 447 48.154 58.076 55.789 1.00 30.39 8 5890 OW0 WAT V 4489.079 102.838 38.708 1.00 30.45 8 5891 OW0 WAT V 449 31.488 67.009 5.9031.00 30.35 8 5892 OW0 WAT V 450 8.486 84.645 16.251 1.00 30.46 8 5893OW0 WAT V 451 17.712 70.200 52.856 1.00 31.30 8 5894 OW0 WAT V 45245.187 54.640 9.218 1.00 30.47 8 5895 OW0 WAT V 453 23.220 65.098 2.0011.00 30.15 8 5896 OW0 WAT V 454 43.353 48.993 23.792 1.00 30.21 8 5897OW0 WAT V 455 0.241 76.716 42.809 1.00 30.43 8 5898 OW0 WAT V 456 38.95490.362 25.885 1.00 31.19 8 5899 OW0 WAT V 457 8.998 51.618 42.193 1.0030.65 8 5900 OW0 WAT V 458 47.484 70.509 20.484 1.00 30.75 8 5901 OW0WAT V 459 26.632 83.732 7.006 1.00 30.86 8 5902 OW0 WAT V 460 27.88784.031 46.702 1.00 31.16 8 5903 OW0 WAT V 461 10.456 52.659 39.931 1.0031.37 8 5904 OW0 WAT V 462 25.474 53.247 11.551 1.00 31.54 8 5905 OW0WAT V 463 21.666 48.674 41.178 1.00 31.71 8 5906 OW0 WAT V 464 51.79963.643 37.234 1.00 30.69 8 5907 OW0 WAT V 465 17.686 48.668 36.134 1.0031.38 8 5908 OW0 WAT V 466 47.081 52.951 49.717 1.00 30.51 8 5909 OW0WAT V 467 15.593 93.203 42.768 1.00 30.90 8 5910 OW0 WAT V 468 36.48080.071 53.771 1.00 30.56 8 5911 OW0 WAT V 469 42.137 47.781 14.882 1.0031.85 8 5912 OW0 WAT V 470 22.333 61.351 70.096 1.00 31.36 8 5913 OW0WAT V 471 40.228 72.527 72.095 1.00 31.17 8 5914 OW0 WAT V 472 1.66674.527 48.132 1.00 31.28 8 5915 OW0 WAT V 473 14.531 66.936 59.718 1.0031.26 8 5916 OW0 WAT V 474 21.000 68.421 1.879 1.00 31.59 8 5917 OW0 WATV 475 37.163 82.170 41.385 1.00 31.32 8 5918 OW0 WAT V 476 26.307 62.0944.445 1.00 31.75 8 5919 OW0 WAT V 477 51.579 61.409 40.641 1.00 31.25 85920 OW0 WAT V 478 41.761 64.533 7.578 1.00 31.59 8 5921 OW0 WAT V 479−7.353 65.632 35.219 1.00 31.13 8 5922 OW0 WAT V 480 16.514 82.72036.237 1.00 31.25 8 5923 OW0 WAT V 481 23.770 75.891 54.586 1.00 31.53 85924 OW0 WAT V 482 50.377 68.458 56.245 1.00 31.72 8 5925 OW0 WAT V 48315.979 105.053 38.501 1.00 30.98 8 5926 OW0 WAT V 484 27.194 93.86731.829 1.00 31.85 8 5927 OW0 WAT V 485 39.487 68.664 5.438 1.00 31.02 85928 OW0 WAT V 486 30.446 58.438 75.573 1.00 31.49 8 5929 OW0 WAT V 487−2.258 85.349 34.418 1.00 31.74 8 5930 OW0 WAT V 488 46.873 56.76965.770 1.00 31.57 8 5931 OW0 WAT V 489 18.407 47.617 19.229 1.00 31.61 85932 OW0 WAT V 490 2.500 78.686 43.392 1.00 31.62 8 5933 OW0 WAT V 4917.727 97.913 42.497 1.00 32.36 8 5934 OW0 WAT V 492 −5.430 71.658 30.9911.00 32.45 8 5935 OW0 WAT V 493 47.547 72.958 21.222 1.00 31.57 8 5936OW0 WAT V 494 9.955 91.961 24.393 1.00 32.43 8 5937 OW0 WAT V 495 12.99652.420 46.232 1.00 31.76 8 5938 OW0 WAT V 496 7.952 65.594 58.841 1.0032.02 8 5939 OW0 WAT V 497 37.204 88.789 33.415 1.00 31.57 8 5940 OW0WAT V 498 36.857 41.938 29.865 1.00 32.38 8 5941 OW0 WAT V 499 7.22051.844 54.727 1.00 32.32 8 5942 OW0 WAT V 500 16.110 76.377 49.777 1.0032.31 8 5943 OW0 WAT V 501 24.511 47.736 42.135 1.00 32.37 8 5944 OW0WAT V 502 22.783 46.357 48.051 1.00 32.64 8 5945 OW0 WAT V 503 27.13860.897 7.569 1.00 32.20 8 5946 OW0 WAT V 504 47.227 50.290 36.850 1.0032.13 8 5947 OW0 WAT V 505 6.733 67.493 23.991 1.00 32.68 8 5948 OW0 WATV 506 16.514 70.176 56.941 1.00 32.03 8 5949 OW0 WAT V 507 43.175 79.6628.514 1.00 31.76 8 5950 OW0 WAT V 508 −3.757 80.394 22.899 1.00 32.62 85951 OW0 WAT V 509 10.932 85.936 45.262 1.00 32.65 8 5952 OW0 WAT V 5103.455 97.650 41.755 1.00 32.31 8 5953 OW0 WAT V 511 33.419 50.551 69.4551.00 32.14 8 5954 OW0 WAT V 512 4.069 99.962 23.550 1.00 33.21 8 5955OW0 WAT V 513 −7.206 65.717 41.690 1.00 33.20 8 5956 OW0 WAT V 51453.785 60.262 61.406 1.00 33.37 8 5957 OW0 WAT V 515 16.599 87.04517.346 1.00 32.99 8 5958 OW0 WAT V 516 47.349 54.074 30.752 1.00 32.14 85959 OW0 WAT V 517 7.038 85.163 42.409 1.00 32.78 8 5960 OW0 WAT V 51816.879 50.503 27.538 1.00 32.69 8 5961 OW0 WAT V 519 30.838 91.77622.385 1.00 33.06 8 5962 OW0 WAT V 520 33.882 41.296 32.218 1.00 34.59 85963 OW0 WAT V 521 53.502 60.512 23.358 1.00 32.27 8 5964 OW0 WAT V 52241.841 73.003 34.316 1.00 33.63 8 5965 OW0 WAT V 523 18.807 69.394 5.3711.00 32.65 8 5966 OW0 WAT V 524 0.567 102.365 27.670 1.00 32.87 8 5967OW0 WAT V 525 28.899 48.822 64.451 1.00 32.62 8 5968 OW0 WAT V 52642.766 46.627 21.339 1.00 33.04 8 5969 OW0 WAT V 527 18.159 66.47260.034 1.00 33.02 8 5970 OW0 WAT V 528 22.385 49.518 59.427 1.00 33.48 85971 OW0 WAT V 529 14.542 53.899 35.438 1.00 32.40 8 5972 OW0 WAT V 5300.923 81.260 18.821 1.00 33.19 8 5973 OW0 WAT V 531 35.980 91.602 25.0731.00 32.89 8 5974 OW0 WAT V 532 40.667 67.024 71.313 1.00 32.79 8 5975OW0 WAT V 533 8.626 61.294 60.713 1.00 32.69 8 5976 OW0 WAT V 534 35.61548.266 53.410 1.00 33.74 8 5977 OW0 WAT V 535 50.581 54.379 41.752 1.0032.75 8 5978 OW0 WAT V 536 34.738 50.213 7.372 1.00 33.68 8 5979 OW0 WATV 537 42.324 79.266 54.340 1.00 32.72 8 5980 OW0 WAT V 538 16.132 78.4418.864 1.00 33.64 8 5981 OW0 WAT V 539 20.256 45.911 20.702 1.00 33.89 85982 OW0 WAT V 540 37.253 43.882 46.170 1.00 33.73 8 5983 OW0 WAT V 54131.158 88.960 12.651 1.00 34.15 8 5984 OW0 WAT V 542 2.885 65.252 30.1821.00 33.66 8 5985 OW0 WAT V 543 24.093 72.008 54.068 1.00 33.53 8 5986OW0 WAT V 544 −4.660 58.902 52.534 1.00 34.13 8 5987 OW0 WAT V 54520.523 52.571 71.335 1.00 34.29 8 5988 OW0 WAT V 546 50.389 70.37343.120 1.00 34.05 8 5989 OW0 WAT V 547 −1.784 74.917 34.717 1.00 34.27 85990 OW0 WAT V 548 25.051 100.468 31.517 1.00 33.73 8 5991 OW0 WAT V 54921.989 83.148 46.194 1.00 34.71 8 5992 OW0 WAT V 550 47.521 62.36411.718 1.00 34.05 8 5993 OW0 WAT V 551 52.236 59.305 62.786 1.00 33.21 85994 OW0 WAT V 552 40.232 80.510 16.448 1.00 34.62 8 5995 OW0 WAT V 55346.253 56.949 70.930 1.00 33.53 8 5996 OW0 WAT V 554 47.895 53.05337.454 1.00 33.41 8 5997 OW0 WAT V 555 13.358 71.030 49.662 1.00 34.43 85998 OW0 WAT V 556 −0.137 73.990 26.087 1.00 34.05 8 5999 OW0 WAT V 55743.973 74.382 6.399 1.00 34.44 8 6000 OW0 WAT V 558 35.593 60.367 77.0221.00 33.63 8 6001 OW0 WAT V 559 6.112 83.592 41.192 1.00 34.97 8 6002OW0 WAT V 560 38.614 41.425 25.492 1.00 34.42 8 6003 OW0 WAT V 56134.074 88.144 12.960 1.00 34.41 8 6004 OW0 WAT V 562 40.114 63.213 5.7861.00 34.56 8 6005 OW0 WAT V 563 −0.202 64.215 60.019 1.00 34.60 8 6006OW0 WAT V 564 4.614 92.264 20.329 1.00 33.82 8 6007 OW0 WAT V 565 15.21250.738 32.687 1.00 34.54 8 6008 OW0 WAT V 566 13.018 70.753 53.378 1.0035.00 8 6009 OW0 WAT V 567 37.836 57.700 75.968 1.00 33.91 8 6010 OW0WAT V 568 18.054 71.354 7.047 1.00 34.28 8 6011 OW0 WAT V 569 20.43557.091 12.782 1.00 34.06 8 6012 OW0 WAT V 570 −1.113 72.836 30.802 1.0034.18 8 6013 OW0 WAT V 571 45.394 47.985 15.576 1.00 34.25 8 6014 OW0WAT V 572 18.083 105.524 25.739 1.00 35.26 8 6015 OW0 WAT V 573 42.36351.035 61.868 1.00 34.64 8 6016 OW0 WAT V 574 3.332 65.717 27.045 1.0035.54 8 6017 OW0 WAT V 575 0.099 70.672 51.291 1.00 34.72 8 6018 OW0 WATV 576 0.045 61.496 31.457 1.00 35.51 8 6019 OW0 WAT V 577 46.395 53.88161.040 1.00 34.53 8 6020 OW0 WAT V 578 52.136 68.150 59.956 1.00 35.10 86021 OW0 WAT V 579 19.009 41.546 26.130 1.00 33.65 8 6022 OW0 WAT V 58034.720 74.712 71.942 1.00 34.54 8 6023 OW0 WAT V 581 37.259 73.78373.743 1.00 35.82 8 6024 OW0 WAT V 582 27.833 55.518 10.945 1.00 34.54 86025 OW0 WAT V 583 46.309 60.566 10.060 1.00 35.04 8 6026 OW0 WAT V 58410.952 63.329 18.773 1.00 34.23 8 6027 OW0 WAT V 585 −1.056 54.48135.620 1.00 34.65 8 6028 OW0 WAT V 586 −4.178 63.600 36.602 1.00 35.48 86029 OW0 WAT V 587 4.690 96.750 20.660 1.00 34.69 8 6030 OW0 WAT V 5888.484 73.376 50.572 1.00 35.07 8 6031 OW0 WAT V 589 44.017 50.506 11.0231.00 35.68 8 6032 OW0 WAT V 590 3.744 50.549 36.911 1.00 35.69 8 6033OW0 WAT V 591 49.672 55.539 26.394 1.00 35.74 8 6034 OW0 WAT V 59227.932 93.666 25.261 1.00 35.64 8 6035 OW0 WAT V 593 22.451 73.99654.266 1.00 35.51 8 6036 OW0 WAT V 594 33.048 48.697 67.743 1.00 35.66 86037 OW0 WAT V 595 12.820 101.046 44.339 1.00 36.16 8 6038 OW0 WAT V 59651.198 69.586 53.643 1.00 35.14 8 6039 OW0 WAT V 597 29.662 79.57454.942 1.00 35.66 8 6040 OW0 WAT V 598 32.247 80.128 52.116 1.00 36.54 86041 OW0 WAT V 599 6.142 51.551 37.685 1.00 35.34 8 6042 OW0 WAT V 6005.622 70.631 22.637 1.00 35.66 8 6043 OW0 WAT V 601 22.365 48.081 48.2421.00 36.08 8 6044 OW0 WAT V 602 8.288 81.332 15.641 1.00 35.59 8 6045OW0 WAT V 603 10.941 74.805 15.117 1.00 35.60 8 6046 OW0 WAT V 60435.796 73.953 1.142 1.00 35.09 8 6047 OW0 WAT V 605 38.777 85.286 9.3091.00 36.46 8 6048 OW0 WAT V 606 20.560 52.963 75.539 1.00 37.03 8 6049OW0 WAT V 607 −3.377 66.230 32.749 1.00 35.54 8 6050 OW0 WAT V 60840.087 44.107 14.031 1.00 36.33 8 6051 OW0 WAT V 609 −1.635 86.95836.864 1.00 35.23 8 6052 OW0 WAT V 610 48.364 69.799 29.088 1.00 35.08 86053 OW0 WAT V 611 18.383 50.939 35.706 1.00 36.23 8 6054 OW0 WAT V 61218.334 58.135 13.735 1.00 37.22 8 6055 OW0 WAT V 613 16.341 55.36950.997 1.00 35.78 8 6056 OW0 WAT V 614 28.580 52.384 12.139 1.00 36.07 86057 OW0 WAT V 615 23.108 103.615 38.927 1.00 36.81 8 6058 OW0 WAT V 61612.325 79.803 46.301 1.00 35.61 8 6059 OW0 WAT V 617 21.280 67.37564.153 1.00 36.55 8 6060 OW0 WAT V 618 40.907 80.214 52.034 1.00 37.09 86061 OW0 WAT V 619 47.006 72.793 58.223 1.00 36.47 8 6062 OW0 WAT V 62020.221 90.473 42.499 1.00 36.27 8 6063 OW0 WAT V 621 4.100 73.674 21.4471.00 36.94 8 6064 OW0 WAT V 622 8.503 104.300 35.973 1.00 36.81 8 6065OW0 WAT V 623 30.691 78.729 57.692 1.00 35.94 8 6066 OW0 WAT V 624−3.070 94.866 30.332 1.00 36.58 8 6067 OW0 WAT V 625 46.455 79.73618.637 1.00 35.97 8 6068 OW0 WAT V 626 46.537 55.701 59.420 1.00 37.10 86069 OW0 WAT V 627 43.765 47.227 50.091 1.00 37.02 8 6070 OW0 WAT V 628−0.451 52.302 37.499 1.00 36.00 8 6071 OW0 WAT V 629 47.301 50.08841.392 1.00 37.12 8 6072 OW0 WAT V 630 37.956 80.815 13.060 1.00 37.94 86073 OW0 WAT V 631 17.138 62.973 7.515 1.00 37.42 8 6074 OW0 WAT V 63213.837 57.372 18.395 1.00 36.82 8 6075 OW0 WAT V 633 41.756 55.82170.896 1.00 36.92 8 6076 OW0 WAT V 634 25.077 93.998 28.706 1.00 36.97 86077 OW0 WAT V 635 47.608 54.704 64.130 1.00 37.13 8 6078 OW0 WAT V 6366.911 105.878 25.141 1.00 36.23 8 6079 OW0 WAT V 637 42.682 67.55769.041 1.00 36.92 8 6080 OW0 WAT V 638 15.363 88.594 48.034 1.00 37.42 86081 OW0 WAT V 639 33.890 42.321 17.015 1.00 37.23 8 6082 OW0 WAT V 6409.736 84.033 43.853 1.00 36.17 8 6083 OW0 WAT V 641 10.886 51.035 46.1031.00 37.66 8 6084 OW0 WAT V 642 27.929 72.978 70.610 1.00 37.35 8 6085OW0 WAT V 643 1.233 69.664 25.786 1.00 37.56 8 6086 OW0 WAT V 644 15.151107.231 33.216 1.00 36.50 8 6087 OW0 WAT V 645 25.823 98.361 30.305 1.0036.65 8 6088 OW0 WAT V 646 34.857 84.394 12.899 1.00 36.71 8 6089 OW0WAT V 647 20.425 52.936 41.877 1.00 36.99 8 6090 OW0 WAT V 648 26.57549.377 65.800 1.00 37.37 8 6091 OW0 WAT V 649 31.193 44.914 15.071 1.0036.96 8 6092 OW0 WAT V 650 10.578 49.772 48.688 1.00 36.01 8 6093 OW0WAT V 651 18.128 51.717 38.409 1.00 37.57 8 6094 OW0 WAT V 652 45.42454.692 56.844 1.00 37.37 8 6095 OW0 WAT V 653 28.011 90.646 18.192 1.0037.91 8 6096 OW0 WAT V 654 47.536 55.043 51.941 1.00 36.73 8 6097 OW0WAT V 655 24.853 98.451 32.915 1.00 37.70 8 6098 OW0 WAT V 656 27.08898.198 26.870 1.00 38.56 8 6099 OW0 WAT V 657 33.663 49.796 11.597 1.0037.19 8 6100 OW0 WAT V 658 16.309 55.242 45.035 1.00 37.83 8 6101 OW0WAT V 659 20.804 43.210 25.195 1.00 37.72 8 6102 OW0 WAT V 660 23.93265.246 70.893 1.00 37.09 8 6103 OW0 WAT V 661 0.664 53.286 53.271 1.0038.36 8 6104 OW0 WAT V 662 40.187 84.151 18.538 1.00 38.05 8 6105 OW0WAT V 663 44.129 77.826 7.095 1.00 38.36 8 6106 OW0 WAT V 664 5.654103.176 36.651 1.00 38.12 8 6107 OW0 WAT V 665 −2.551 55.092 37.581 1.0039.63 8 6108 OW0 WAT V 666 48.102 56.702 13.267 1.00 37.64 8 6109 OW0WAT V 667 27.824 90.475 15.555 1.00 36.41 8 6110 OW0 WAT V 668 38.69949.812 63.112 1.00 37.80 8 6111 OW0 WAT V 669 −2.199 54.401 53.588 1.0039.21 8 6112 OW0 WAT V 670 19.006 53.240 47.228 1.00 38.93 8 6113 OW0WAT V 671 46.897 48.817 19.829 1.00 39.11 8 6114 OW0 WAT V 672 42.30148.935 12.664 1.00 37.43 8 6115 OW0 WAT V 673 16.098 53.972 53.322 1.0038.55 8 6116 OW0 WAT V 674 16.992 66.360 61.965 1.00 40.47 8 6117 OW0WAT V 675 17.396 84.259 14.592 1.00 37.45 8 6118 OW0 WAT V 676 48.02370.300 38.414 1.00 38.28 8 6119 OW0 WAT V 677 21.061 60.355 72.008 1.0038.68 8 6120 OW0 WAT V 678 25.412 45.777 15.102 1.00 40.05 8 6121 OW0WAT V 679 43.705 73.272 1.624 1.00 38.78 8 6122 OW0 WAT V 680 17.37967.334 7.173 1.00 38.88 8 6123 OW0 WAT V 681 19.500 72.583 5.113 1.0041.12 8 6124 OW0 WAT V 682 27.135 53.269 75.096 1.00 38.74 8 6125 OW0WAT V 683 43.871 76.670 2.397 1.00 38.42 8 6126 OW0 WAT V 684 32.69047.277 60.342 1.00 38.23 8 6127 OW0 WAT V 685 38.889 50.643 67.387 1.0038.05 8 6128 OW0 WAT V 686 15.848 75.816 7.403 1.00 37.86 8 6129 OW0 WATV 687 25.036 96.149 30.003 1.00 38.02 8 6130 OW0 WAT V 688 44.120 49.14754.661 1.00 39.21 8 6131 OW0 WAT V 689 31.793 51.208 10.937 1.00 39.53 86132 OW0 WAT V 690 9.476 96.492 43.783 1.00 37.31 8 6133 OW0 WAT V 6918.821 88.129 44.638 1.00 39.95 8 6134 OW0 WAT V 692 8.003 80.636 43.6441.00 37.70 8 6135 OW0 WAT V 693 14.834 83.314 13.883 1.00 39.80 8 6136OW0 WAT V 694 21.370 44.389 41.265 1.00 39.75 8 6137 OW0 WAT V 69525.208 85.122 7.995 1.00 38.90 8 6138 OW0 WAT V 696 34.431 64.498 5.8821.00 37.43 8 6139 OW0 WAT V 697 46.857 48.623 44.260 1.00 38.67 8 6140OW0 WAT V 698 48.394 49.074 31.806 1.00 38.40 8 6141 OW0 WAT V 699 6.33071.875 18.323 1.00 39.24 8 6142 OW0 WAT V 700 3.567 68.493 56.513 1.0039.03 8 6143 OW0 WAT V 701 19.531 67.580 61.273 1.00 38.68 8 6144 OW0WAT V 702 36.514 82.654 34.129 1.00 38.10 8 6145 OW0 WAT V 703 43.55950.161 59.718 1.00 39.15 8 6146 OW0 WAT V 704 41.881 70.064 7.497 1.0039.49 8 6147 OW0 WAT V 705 12.039 106.892 30.442 1.00 39.69 8 6148 OW0WAT V 706 25.673 81.581 52.252 1.00 39.17 8 6149 OW0 WAT V 707 46.85574.915 26.181 1.00 40.35 8 6150 OW0 WAT V 708 21.077 93.052 39.231 1.0039.44 8 6151 OW0 WAT V 709 28.621 62.328 5.470 1.00 38.56 8 6152 OW0 WATV 710 −3.607 57.742 54.506 1.00 38.82 8 6153 OW0 WAT V 711 25.913 41.71429.843 1.00 38.94 8 6154 OW0 WAT V 712 21.385 95.763 42.160 1.00 39.85 86155 OW0 WAT V 713 39.666 46.565 56.093 1.00 40.16 8 6156 OW0 WAT V 71433.043 47.398 12.747 1.00 38.56 8 6157 OW0 WAT V 715 3.335 48.480 47.5231.00 40.24 8 6158 OW0 WAT V 716 −5.954 59.355 43.289 1.00 39.30 8 6159OW0 WAT V 717 −2.633 70.380 52.100 1.00 39.49 8 6160 OW0 WAT V 71814.943 51.881 28.927 1.00 41.17 8 6161 OW0 WAT V 719 30.665 55.78976.270 1.00 36.29 8 6162 OW0 WAT V 720 38.153 41.243 44.336 1.00 39.61 86163 OW0 WAT V 721 42.857 72.924 4.760 1.00 39.33 8 6164 OW0 WAT V 72242.983 45.506 30.086 1.00 39.35 8 6165 OW0 WAT V 723 8.541 68.671 15.4771.00 40.10 8 6166 OW0 WAT V 724 3.357 68.745 24.682 1.00 39.21 8 6167OW0 WAT V 725 32.096 74.899 2.155 1.00 38.68 8 6168 OW0 WAT V 726 −3.31699.677 31.930 1.00 40.29 8 6169 OW0 WAT V 727 33.290 44.355 45.552 1.0039.94 8 6170 OW0 WAT V 728 50.677 69.314 25.213 1.00 38.89 8 6171 OW0WAT V 729 35.441 42.395 37.048 1.00 39.29 8 6172 OW0 WAT V 730 8.36353.922 35.516 1.00 38.32 8 6173 OW0 WAT V 731 −1.713 91.588 39.071 1.0040.09 8 6174 OW0 WAT V 732 22.068 82.950 49.452 1.00 38.86 8 6175 OW0WAT V 733 −1.449 89.011 21.652 1.00 39.99 8 6176 OW0 WAT V 734 37.35459.035 5.289 1.00 40.90 8 6177 OW0 WAT V 735 20.992 87.687 45.698 1.0040.19 8 6178 OW0 WAT V 736 46.650 76.726 54.492 1.00 40.47 8 6179 OW0WAT V 737 7.370 47.777 49.173 1.00 41.37 8 6180 OW0 WAT V 738 14.27971.404 55.742 1.00 39.06 8 6181 OW0 WAT V 739 13.276 62.067 63.468 1.0038.95 8 6182 OW0 WAT V 740 47.469 55.262 33.788 1.00 41.14 8 6183 OW0WAT V 741 35.182 72.963 73.409 1.00 38.69 8 6184 OW0 WAT V 742 28.99342.749 41.796 1.00 40.22 8 6185 OW0 WAT V 743 12.430 51.804 37.400 1.0039.68 8 6186 OW0 WAT V 744 5.325 85.408 18.950 1.00 41.26 8 6187 OW0 WATV 745 41.721 66.169 73.677 1.00 39.43 8 6188 OW0 WAT V 746 16.983 83.51910.040 1.00 40.83 8 6189 OW0 WAT V 747 −3.245 67.552 51.568 1.00 41.14 86190 OW0 WAT V 748 18.547 72.699 54.390 1.00 40.80 8 6191 OW0 WAT V 74950.952 65.503 10.665 1.00 39.71 8 6192 OW0 WAT V 750 6.873 59.618 31.0971.00 40.61 8 6193 OW0 WAT V 751 44.643 72.249 41.540 1.00 40.21 8 6194OW0 WAT V 752 10.333 59.620 21.158 1.00 40.03 8 6195 OW0 WAT V 75325.342 99.843 20.985 1.00 40.88 8 6196 OW0 WAT V 754 13.886 67.34151.913 1.00 41.40 8 6197 OW0 WAT V 755 20.669 50.466 56.076 1.00 40.93 86198 OW0 WAT V 756 16.062 51.352 42.439 0.00 41.08 8 6199 OW0 WAT V 757−2.323 91.095 34.519 1.00 40.69 8 6200 OW0 WAT V 758 3.987 63.229 29.3531.00 41.53 8 6201 OW0 WAT V 759 20.694 99.900 18.786 1.00 39.84 8 6202OW0 WAT V 760 21.098 72.115 58.710 1.00 40.04 8 6203 OW0 WAT V 76139.451 41.349 13.513 1.00 40.57 8 6204 OW0 WAT V 762 3.185 80.792 42.0001.00 41.27 8 6205 OW0 WAT V 763 15.866 68.494 52.407 1.00 40.90 8 6206OW0 WAT V 764 42.027 79.686 47.257 1.00 40.14 8 6207 OW0 WAT V 76541.063 55.022 68.081 1.00 42.98 8 6208 OW0 WAT V 766 15.728 85.26116.175 1.00 42.08 8 6209 OW0 WAT V 767 −8.665 63.541 41.234 1.00 40.98 86210 OW0 WAT V 768 28.828 85.580 44.440 1.00 40.75 8 6211 OW0 WAT V 76946.504 46.346 43.773 1.00 40.98 8 6212 OW0 WAT V 770 52.964 61.42954.373 1.00 41.49 8 6213 OW0 WAT V 771 25.001 95.005 39.507 1.00 41.35 86214 OW0 WAT V 772 4.818 62.633 59.449 1.00 41.54 8 6215 OW0 WAT V 77318.916 60.160 66.080 1.00 41.09 8 6216 OW0 WAT V 774 27.033 88.84112.019 1.00 41.39 8 6217 OW0 WAT V 775 13.803 67.385 57.044 1.00 41.01 86218 OW0 WAT V 776 11.356 101.651 18.715 1.00 42.40 8 6219 OW0 WAT V 77750.379 57.839 57.286 1.00 38.80 8 6220 OW0 WAT V 778 9.739 81.288 44.9911.00 38.14 8 6221 OW0 WAT V 779 26.770 45.470 44.155 1.00 39.31 8 6222OW0 WAT V 780 51.219 61.900 12.424 1.00 42.17 8 6223 OW0 WAT V 78144.665 53.194 62.632 1.00 40.09 8 6224 OW0 WAT V 782 −4.332 57.89145.992 1.00 43.38 8 6225 OW0 WAT V 783 54.313 63.995 27.513 1.00 40.34 86226 OW0 WAT V 784 26.835 56.319 8.446 1.00 41.42 8 6227 OW0 WAT V 78553.198 59.584 25.852 1.00 42.12 8 6228 OW0 WAT V 786 19.476 44.84523.558 1.00 42.02 8 6229 OW0 WAT V 787 21.294 88.109 18.755 1.00 42.02 86230 OW0 WAT V 788 46.461 57.071 56.124 1.00 41.88 8 6231 OW0 WAT V 78952.975 62.124 50.393 1.00 41.59 8 6232 OW0 WAT V 790 8.480 108.23524.221 1.00 42.16 8 6233 OW0 WAT V 791 18.517 78.200 51.474 1.00 42.31 86234 OW0 WAT V 792 −5.150 51.726 49.471 1.00 40.85 8 6235 OW0 WAT V 79336.849 55.447 72.633 1.00 42.13 8 6236 OW0 WAT V 794 37.563 79.69442.494 1.00 41.67 8 6237 OW0 WAT V 795 18.818 84.285 16.222 1.00 43.03 86238 OW0 WAT V 796 36.451 82.759 13.933 1.00 41.71 8 6239 OW0 WAT V 79722.906 51.457 67.808 1.00 41.33 8 6240 OW0 WAT V 798 1.528 102.17136.053 1.00 41.41 8 6241 OW0 WAT V 799 36.684 45.294 51.188 1.00 42.88 86242 OW0 WAT V 800 14.017 67.414 9.706 1.00 41.87 8 6243 OW0 WAT V 80147.832 66.788 18.650 1.00 43.94 8 6244 OW0 WAT V 802 34.436 88.32436.102 1.00 43.03 8 6245 OW0 WAT V 803 24.260 67.815 69.741 1.00 42.57 86246 OW0 WAT V 804 13.129 74.685 52.293 1.00 42.14 8 6247 OW0 WAT V 80516.572 61.433 12.722 1.00 41.61 8 6248 OW0 WAT V 806 46.827 51.42947.524 1.00 42.73 8 6249 OW0 WAT V 807 26.546 48.730 71.404 1.00 42.47 86250 OW0 WAT V 808 33.308 76.572 61.813 1.00 42.82 8 6251 OW0 WAT V 80916.314 98.564 17.363 1.00 42.43 8 6252 OW0 WAT V 810 47.038 73.62061.642 1.00 43.62 8 6253 OW0 WAT V 811 23.301 74.541 1.386 1.00 44.52 86254 OW0 WAT V 812 23.719 88.481 37.683 1.00 40.46 8 6255 OW0 WAT V 81331.440 60.185 76.751 1.00 43.11 8 6256 OW0 WAT V 814 16.573 101.55019.316 1.00 43.14 8 6257 OW0 WAT V 815 4.201 55.069 57.571 1.00 42.80 86258 OW0 WAT V 816 −5.755 72.609 47.268 1.00 41.92 8 6259 OW0 WAT V 81723.802 106.033 28.040 1.00 42.13 8 6260 OW0 WAT V 818 28.580 91.42735.569 1.00 44.77 8 6261 OW0 WAT V 819 −6.927 74.495 44.783 1.00 42.39 86262 OW0 WAT V 820 42.898 80.745 21.282 1.00 42.72 8 6263 OW0 WAT V 82144.594 48.996 19.414 1.00 42.65 8 6264 OW0 WAT V 822 22.357 66.60868.417 1.00 43.63 8 6265 OW0 WAT V 823 25.576 50.604 10.991 1.00 43.85 86266 OW0 WAT V 824 47.220 77.741 25.726 1.00 44.91 8 6267 OW0 WAT V 82516.600 55.517 47.156 1.00 44.33 8 6268 OW0 WAT V 826 1.892 50.074 39.1161.00 42.83 8 6269 OW0 WAT V 827 24.440 89.039 35.388 1.00 43.51 8 6270OW0 WAT V 828 21.480 53.418 43.918 1.00 43.38 8 6271 OW0 WAT V 82914.604 82.502 11.170 1.00 41.84 8 6272 OW0 WAT V 830 14.875 62.76514.779 1.00 42.12 8 6273 OW0 WAT V 831 3.701 80.451 16.127 1.00 43.54 86274 OW0 WAT V 832 48.724 69.957 34.245 1.00 43.72 8 6275 OW0 WAT V 83333.297 59.385 78.143 1.00 45.08 8 6276 OW0 WAT V 834 17.544 53.59351.513 1.00 46.32 8 6277 OW0 WAT V 835 12.009 85.638 47.505 1.00 44.72 86278 OW0 WAT V 836 12.936 54.854 19.146 1.00 42.89 8 6279 OW0 WAT V 83724.005 43.446 16.058 1.00 42.88 8 6280 OW0 WAT V 838 2.563 57.015 61.4061.00 42.80 8 6281 OW0 WAT V 839 17.292 81.361 47.327 1.00 43.05 8 6282OW0 WAT V 840 26.973 97.353 24.292 1.00 42.44 8 6283 OW0 WAT V 84124.520 83.741 45.252 1.00 44.48 8 6284 OW0 WAT V 842 40.943 89.45222.148 1.00 43.11 8 6285 OW0 WAT V 843 17.748 68.046 54.218 1.00 43.50 86286 OW0 WAT V 844 53.072 63.513 23.413 1.00 44.03 8 6287 OW0 WAT V 845−1.018 97.468 34.805 1.00 44.47 8 6288 OW0 WAT V 846 14.885 69.98910.290 1.00 44.92 8 6289 OW0 WAT V 847 15.800 50.802 20.677 1.00 46.01 86290 OW0 WAT V 848 25.982 102.118 29.899 1.00 44.94 8 6291 OW0 WAT V 8490.247 52.205 55.531 1.00 45.62 8 6292 OW0 WAT V 850 18.884 61.154 6.1321.00 44.78 8 6293 OW0 WAT V 851 11.959 71.909 12.344 1.00 44.89 8 6294OW0 WAT V 852 −1.246 74.512 28.721 1.00 43.38 8 6295 OW0 WAT V 85339.883 48.418 12.157 1.00 44.97 8 6296 OW0 WAT V 854 25.484 65.08275.271 1.00 40.98 8 6297 OW0 WAT V 855 31.943 70.931 74.851 1.00 43.51 86298 OW0 WAT V 856 35.277 49.445 9.697 1.00 45.37 8 6299 OW0 WAT V 85751.902 64.035 51.472 1.00 44.46 8 6300 OW0 WAT V 858 5.381 94.650 19.2921.00 45.20 8 6301 OW0 WAT V 859 14.161 52.807 19.941 1.00 44.99 8 6302OW0 WAT V 860 0.976 49.582 46.683 1.00 45.54 8 6303 OW0 WAT V 861 11.37856.649 26.955 1.00 46.98 8 6304 OW0 WAT V 862 23.725 48.499 52.657 1.0043.58 8 6305 OW0 WAT V 863 31.619 53.767 4.982 1.00 44.03 8 6306 OW0 WATV 864 21.564 85.158 16.121 1.00 46.34 8 6307 OW0 WAT V 865 48.454 57.83331.207 1.00 45.05 8 6308 OW0 WAT V 866 13.820 78.070 11.134 1.00 47.52 86309 OW0 WAT V 867 53.268 61.611 27.715 1.00 45.47 8 6310 OW0 WAT V 86840.661 42.455 21.732 1.00 43.57 8 6311 OW0 WAT V 869 24.881 97.60917.754 1.00 41.56 8 6312 OW0 WAT V 870 46.779 45.863 33.183 1.00 38.06 86313 OW0 WAT V 871 28.449 47.238 49.410 1.00 44.98 8 6314 OW0 WAT V 87231.691 90.618 16.034 1.00 45.59 8 6315 OW0 WAT V 873 45.269 73.27125.041 1.00 46.87 8 6316 OW0 WAT V 874 18.096 50.245 53.261 1.00 45.09 86317 OW0 WAT V 875 −5.062 64.679 39.520 1.00 44.00 8 6318 OW0 WAT V 87617.006 54.092 49.423 1.00 46.50 8 6319 OW0 WAT V 877 39.580 64.10777.580 1.00 45.16 8 6320 OW0 WAT V 878 16.405 56.330 66.595 1.00 44.67 86321 OW0 WAT V 879 28.253 74.829 0.308 1.00 44.14 8 6322 OW0 WAT V 88026.165 96.027 33.730 1.00 45.73 8 6323 OW0 WAT V 881 25.024 94.67331.684 1.00 45.30 8 6324 OW0 WAT V 882 6.382 101.590 23.078 1.00 45.88 86325 OW0 WAT V 883 20.784 106.032 25.469 1.00 44.92 8 6326 OW0 WAT V 88415.678 70.001 59.741 1.00 47.72 8 6327 OW0 WAT V 885 43.426 78.17561.043 1.00 46.23 8 6328 OW0 WAT V 886 10.651 50.358 43.666 1.00 45.79 86329 OW0 WAT V 887 0.918 49.811 54.685 1.00 45.38 8 6330 OW0 WAT V 88824.371 106.460 30.607 1.00 46.20 8 6331 OW0 WAT V 889 7.425 93.59016.782 1.00 45.79 8 6332 OW0 WAT V 890 20.314 66.093 66.469 1.00 48.35 86333 OW0 WAT V 891 12.244 93.829 44.935 1.00 47.03 8 6334 OW0 WAT V 8922.847 56.085 32.137 1.00 48.09 8 6335 OW0 WAT V 893 15.592 72.473 53.5881.00 46.24 8 6336 OW0 WAT V 894 45.552 49.673 29.081 1.00 46.73 8 6337OW0 WAT V 895 48.867 72.566 56.249 1.00 45.76 8 6338 OW0 WAT V 89651.123 56.932 37.786 1.00 40.59 8 6339 OW0 WAT V 897 30.394 49.733 9.1421.00 48.10 8 6340 OW0 WAT V 898 27.101 98.920 22.257 1.00 46.90 8 6341OW0 WAT V 899 14.712 51.617 24.308 1.00 47.17 8 6342 OW0 WAT V 90046.781 50.533 27.214 1.00 47.00 8 6343 OW0 WAT W 1 −6.114 65.250 32.6691.00 47.96 8 6344 OW0 WAT W 2 47.645 71.480 60.598 1.00 45.49 8 6345 OW0WAT W 3 48.802 54.151 54.398 1.00 46.37 8 6346 OW0 WAT W 4 4.605 105.26826.990 1.00 46.92 8 6347 OW0 WAT W 5 42.143 73.136 41.061 1.00 45.02 86348 OW0 WAT W 6 26.105 89.154 41.563 1.00 47.90 8 6349 OW0 WAT W 73.202 48.853 55.140 1.00 47.23 8 6350 OW0 WAT W 8 −2.318 61.724 33.4581.00 48.00 8 6351 OW0 WAT W 9 38.569 50.803 7.204 1.00 46.95 8 6352 OW0WAT W 10 2.160 103.336 25.390 1.00 47.08 8 6353 OW0 WAT W 11 27.46441.903 36.189 1.00 42.96 8 6354 OW0 WAT W 12 49.209 50.152 22.583 1.0048.25 8 6355 OW0 WAT W 13 10.266 57.487 62.131 1.00 43.39 8 6356 OW0 WATW 14 54.127 66.185 63.244 1.00 49.78 8 6357 OW0 WAT W 15 19.083 49.33063.179 1.00 49.30 8 6358 OW0 WAT W 16 39.385 74.287 38.793 1.00 46.50 86359 OW0 WAT W 17 −1.255 52.062 41.948 1.00 49.09 8 6360 OW0 WAT W 1816.630 69.708 8.569 1.00 48.63 8 6361 OW0 WAT W 19 29.289 54.314 9.2081.00 49.09 8 6362 OW0 WAT W 20 38.590 83.950 31.916 1.00 48.14 8 6363OW0 WAT W 21 47.212 44.923 37.558 1.00 49.07 8 6364 OW0 WAT W 22 2.016104.557 33.998 1.00 50.31 8 6365 OW0 WAT W 23 5.910 79.410 15.810 1.0046.74 8 6366 OW0 WAT W 24 18.824 46.920 16.693 1.00 44.54 8 6367 OW0 WATW 25 21.253 90.457 18.335 1.00 47.12 8 6368 OW0 WAT W 26 46.674 72.57634.746 1.00 48.69 8 6369 OW0 WAT W 27 17.804 54.470 14.884 1.00 50.05 86370 OW0 WAT W 28 −3.319 64.779 54.655 1.00 49.95 8 6371 OW0 WAT W 2920.035 59.810 69.328 1.00 47.36 8 6372 OW0 WAT W 30 6.598 98.214 19.5291.00 50.29 8 6373 OW0 WAT W 31 29.388 57.634 5.275 1.00 49.23 8 6374 OW0WAT W 32 25.881 83.371 49.453 1.00 49.89 8 6375 OW0 WAT W 33 46.82848.534 13.616 1.00 48.17 8 6376 OW0 WAT W 34 52.912 62.999 14.852 1.0046.56 8 6377 OW0 WAT W 35 2.107 83.103 18.070 1.00 48.10 8 6378 OW0 WATW 36 41.486 67.797 7.736 1.00 50.23 8 6379 OW0 WAT W 37 9.492 94.96215.817 1.00 48.00 8 6380 OW0 WAT W 38 28.348 95.134 21.001 1.00 48.19 86381 OW0 WAT W 39 32.401 92.434 25.439 1.00 50.58 8 6382 OW0 WAT W 4046.035 46.956 48.050 1.00 50.92 8 6383 OW0 WAT W 41 34.909 51.572 71.1591.00 49.38 8 6384 OW0 WAT W 42 29.114 76.486 61.672 1.00 49.83 8 6385OW0 WAT W 43 −3.044 91.942 40.975 1.00 51.92 8 6386 OW0 WAT W 44 −3.39574.451 28.328 1.00 46.84 8 6387 OW0 WAT W 45 20.187 89.421 44.602 1.0049.88 8 6388 OW0 WAT W 46 −4.080 54.699 41.545 1.00 50.13 8 6389 OW0 WATW 47 38.425 87.733 31.621 1.00 49.47 8 6390 OW0 WAT W 48 4.305 62.41362.323 1.00 49.60 8 6391 OW0 WAT W 49 6.229 89.367 44.095 1.00 53.06 86392 OW0 WAT W 50 49.747 66.902 23.155 0.00 51.47 8 6393 OW0 WAT W 5140.855 78.417 26.292 1.00 48.79 8 6394 OW0 WAT W 52 17.489 50.714 66.8951.00 52.19 8 6395 OW0 WAT W 53 34.327 92.622 27.782 1.00 49.40 8 6396OW0 WAT W 54 49.464 48.219 14.354 1.00 55.58 8 6397 OW0 WAT W 55 −2.82349.394 48.028 1.00 50.11 8 6398 OW0 WAT W 56 22.263 105.611 23.242 1.0050.89 8 6399 OW0 WAT W 57 16.395 51.479 56.998 1.00 54.48 8 6400 OW0 WATW 58 46.461 51.028 12.082 1.00 51.52 8 6401 OW0 WAT W 59 35.996 61.6515.602 1.00 53.96 8 6402 OW0 WAT W 60 25.277 46.888 50.958 1.00 53.30 86403 OW0 WAT W 61 15.763 94.604 17.487 1.00 49.77 8 6404 OW0 WAT W 6242.937 61.534 7.934 1.00 47.74 8 6405 OW0 WAT W 63 24.840 46.516 44.0721.00 51.69 8 6406 OW0 WAT W 64 29.111 92.028 40.197 1.00 48.35 8 6407OW0 WAT W 65 4.689 89.221 19.393 1.00 50.44 8 6408 OW0 WAT W 66 11.45693.383 15.046 1.00 58.07 8 6409 OW0 WAT W 67 15.227 108.500 35.816 1.0052.43 8 6410 OW0 WAT W 68 42.860 74.904 32.815 1.00 52.70 8 6411 OW0 WATW 69 48.829 69.006 23.605 1.00 55.19 8 6412 OW0 WAT W 70 15.485 68.66611.962 1.00 52.48 8 6413 OW0 WAT W 71 −5.047 98.836 30.411 1.00 52.33 86414 OW0 WAT W 72 38.899 69.928 3.024 1.00 53.43 8 6415 OW0 WAT W 7347.563 47.253 16.948 1.00 53.16 8 6416 OW0 WAT W 74 8.621 51.721 57.8101.00 51.63 8 6417 OW0 WAT W 75 52.887 59.020 49.147 1.00 50.28 8 6418OW0 WAT W 76 4.037 61.529 30.846 1.00 54.62 8 6419 OW0 WAT W 77 4.33283.232 16.091 1.00 55.82 8 6420 OW0 WAT W 78 36.037 53.977 74.978 1.0055.15 8 6421 OW0 WAT W 79 51.512 53.978 47.701 0.00 54.18 8 6422 OW0 WATW 80 14.797 91.920 17.273 1.00 51.87 8 6423 OW0 WAT W 81 19.801 84.3698.356 1.00 55.63 8 6424 OW0 WAT W 82 31.496 46.252 52.107 1.00 55.15 86425 OW0 WAT W 83 −1.823 79.829 19.762 1.00 53.76 8 6426 OW0 WAT W 8429.256 92.834 20.731 1.00 53.49 8 6427 OW0 WAT W 85 −1.824 76.279 32.5631.00 55.76 8 6428 OW0 WAT W 86 32.061 46.088 49.588 1.00 55.95 8 6429OW0 WAT W 87 41.327 42.439 33.669 1.00 55.86 8 6430 OW0 WAT W 88 43.15380.324 3.532 1.00 52.67 8 6431 OW0 WAT W 89 47.799 76.801 61.841 1.0055.93 8 6432 OW0 WAT W 90 35.708 85.333 37.348 1.00 54.64 8 6433 OW0 WATW 91 52.110 65.452 56.038 1.00 53.77 8 6434 OW0 WAT W 92 16.996 79.16747.458 1.00 56.65 8 6435 OW0 WAT W 93 27.626 49.502 11.515 1.00 60.46 86436 OW0 WAT W 94 29.317 47.547 14.906 1.00 61.23 8 6437 OW0 WAT W 9551.306 65.455 30.794 0.00 67.31 8 6438 OW0 WAT W 96 21.436 52.799 12.4751.00 60.39 8 6439 OW0 WAT W 97 24.857 50.122 68.228 1.00 61.97 8 6440OW0 WAT W 98 53.436 60.942 47.809 1.00 59.88 8 6441 OW0 WAT W 99 26.54599.863 28.613 1.00 66.13 8 6442 OW0 WAT W 100 28.187 94.100 34.809 1.0047.55 8 6443 OW0 WAT W 101 46.501 68.477 9.327 1.00 62.49 8 6444 OW0 WATW 102 41.335 80.622 32.546 1.00 56.46 8 6445 OW0 WAT W 103 49.090 47.01929.937 1.00 51.60 8 6446 OW0 WAT W 104 29.677 70.505 75.480 1.00 55.52 86447 OW0 WAT W 105 10.580 70.552 56.020 1.00 45.60 8 6448 OW0 WAT W 106−5.437 61.460 36.195 1.00 49.58 8 6449 OW0 WAT W 107 41.636 42.37828.372 1.00 47.73 8 6450 OW0 WAT W 108 48.134 51.375 29.584 1.00 53.67 86451 OW0 WAT W 109 20.029 46.534 41.141 1.00 45.69 8 6452 OW0 WAT W 11039.076 61.857 77.827 1.00 61.24 8 6453 OW0 WAT W 111 40.140 79.60228.296 1.00 58.08 8 6454 OW0 WAT W 112 24.479 41.686 38.003 1.00 48.71 86455 OW0 WAT W 113 18.748 86.522 18.736 1.00 54.95 8 6456 OW0 WAT W 11426.670 86.155 43.878 1.00 45.83 8 6457 OW0 WAT W 115 34.014 44.10158.947 1.00 55.80 8 6458 OW0 WAT W 116 44.085 44.358 32.579 1.00 66.42 86459 OW0 WAT W 117 2.549 102.526 41.260 1.00 56.37 8 6460 OW0 WAT W 11810.042 59.115 64.251 1.00 53.53 8 6461 OW0 WAT W 119 52.498 59.27137.676 1.00 46.44 8 6462 OW0 WAT W 120 49.412 68.479 30.738 0.00 48.32 86463 OW0 WAT W 121 39.604 81.174 29.899 1.00 40.72 8 6464 OW0 WAT W 12252.578 62.726 30.463 0.00 55.27 8 6465 OW0 WAT W 123 32.284 38.99232.423 1.00 44.19 8 6466 OW0 WAT W 124 54.342 58.298 13.900 1.00 48.84 86467 OW0 WAT W 125 53.831 60.018 17.609 1.00 53.12 8 6468 OW0 WAT W 12637.548 48.910 67.790 1.00 63.29 8 6469 OW0 WAT W 127 16.364 67.20164.210 1.00 54.77 8 6470 OW0 WAT W 128 35.507 88.726 18.930 1.00 44.18 86471 OW0 WAT W 129 49.585 56.011 59.240 1.00 44.54 8 6472 OW0 WAT W 13013.470 54.095 28.765 1.00 39.17 8 6473 OW0 WAT W 131 11.141 90.68016.198 1.00 49.46 8 6474 OW0 WAT W 132 −9.184 65.150 46.616 1.00 52.99 86475 OW0 WAT W 133 44.910 67.182 7.757 1.00 52.67 8 6476 OW0 WAT W 13438.968 68.370 71.252 1.00 37.18 8 6477 OW0 WAT W 135 9.962 106.66135.598 1.00 48.81 8 6478 OW0 WAT W 136 −0.018 83.329 37.562 1.00 49.93 86479 OW0 WAT W 137 6.077 95.625 42.890 1.00 41.31 8 6480 OW0 WAT W 13838.033 48.935 8.928 1.00 56.21 8 6481 OW0 WAT W 139 22.720 48.167 43.4061.00 43.05 8 6482 OW0 WAT W 140 16.160 51.440 42.398 1.00 42.33 8 6483OW0 WAT W 141 51.286 65.520 30.747 0.00 58.93 8 6484 OW0 WAT W 14222.870 83.783 −0.279 1.00 39.91 8 6485 OW0 WAT W 143 23.492 85.41114.742 1.00 45.55 8 6486 OW0 WAT W 144 30.609 38.135 34.869 1.00 53.23 86487 OW0 WAT W 145 51.546 53.971 47.725 0.00 54.90 8 6488 OW0 WAT W 14637.344 40.493 33.234 1.00 46.02 8 6489 OW0 WAT W 147 35.805 47.57262.190 1.00 53.24 8 6490 OW0 WAT W 148 32.439 62.293 76.111 1.00 52.51 86491 OW0 WAT W 149 24.077 90.751 37.673 1.00 48.00 8 6492 OW0 WAT W 15020.655 50.869 68.464 1.00 51.34 8 6493 OW0 WAT W 151 42.359 76.80031.368 1.00 54.68 8 6494 OW0 WAT W 152 40.991 84.869 28.522 1.00 51.94 86495 OW0 WAT W 153 −3.448 59.486 34.298 1.00 60.14 8 6496 OW0 WAT W 15424.275 50.044 65.629 1.00 48.99 8 6497 OW0 WAT W 155 24.898 47.63557.042 1.00 50.00 8 6498 OW0 WAT W 156 46.911 73.376 32.086 1.00 65.97 86499 OW0 WAT W 157 12.448 63.643 14.806 1.00 50.68 8 6500 OW0 WAT W 15817.367 83.516 7.750 1.00 59.03 8 6501 OW0 WAT W 159 38.537 87.429 19.2441.00 48.05 8 6502 OW0 WAT W 160 49.397 68.482 30.753 0.00 47.12 8 6503OW0 WAT W 161 52.562 62.737 30.460 0.00 55.04 8 6504 OW0 WAT W 16217.100 92.730 17.506 1.00 48.89 8 6505 OW0 WAT W 163 54.143 65.66653.272 1.00 49.78 8 6506 OW0 WAT W 164 35.140 89.217 21.335 0.00 49.55 86507 OW0 WAT W 165 40.864 85.144 25.201 1.00 51.96 8 6508 OW0 WAT W 1660.129 71.062 53.859 1.00 50.46 8 6509 OW0 WAT W 167 19.749 95.732 16.3951.00 54.02 8 6510 OW0 WAT W 168 45.089 55.696 66.763 1.00 48.69 8 6511OW0 WAT W 169 29.920 93.952 27.969 1.00 57.82 8 6512 OW0 WAT W 170−1.140 103.281 29.038 1.00 59.68 8 6513 OW0 WAT W 171 0.493 67.33227.261 1.00 46.75 8 6514 OW0 WAT W 172 11.663 49.273 52.961 1.00 47.65 86515 OW0 WAT W 173 19.395 43.670 27.526 0.00 52.64 8 6516 OW0 WAT W 17412.558 73.429 10.221 1.00 52.09 8 6517 OW0 WAT W 175 47.725 72.16825.475 1.00 55.03 8 6518 OW0 WAT W 176 37.354 46.525 53.992 1.00 62.86 86519 OW0 WAT W 177 6.566 77.689 48.060 1.00 54.04 8 6520 OW0 WAT W 17827.239 80.756 54.362 1.00 54.49 8 6521 OW0 WAT W 179 29.136 79.11559.854 1.00 51.47 8 6522 OW0 WAT W 180 51.301 65.512 30.778 1.00 58.87 86523 OW0 WAT W 181 49.729 67.077 23.232 1.00 50.64 8 6524 OW0 WAT W 18215.428 63.127 65.725 1.00 53.21 8 6525 OW0 WAT W 183 28.316 47.47359.001 1.00 52.58 8 6526 OW0 WAT W 184 11.167 50.777 21.789 1.00 55.21 86527 OW0 WAT W 185 39.667 45.779 11.484 1.00 50.46 8 6528 OW0 WAT W 1869.302 78.481 48.408 1.00 50.14 8 6529 OW0 WAT W 187 −2.511 95.777 25.0821.00 50.26 8 6530 OW0 WAT W 188 49.525 52.221 41.616 1.00 53.78 8 6531OW0 WAT W 189 33.219 90.787 32.195 1.00 53.22 8 6532 OW0 WAT W 19018.629 63.971 67.355 1.00 54.97 8 6533 OW0 WAT W 191 6.996 55.402 34.7901.00 49.49 8 6534 OW0 WAT W 192 50.269 70.807 60.070 1.00 54.80 8 6535OW0 WAT W 193 −3.948 89.479 31.518 0.00 54.80 8 6536 OW0 WAT W 194 4.03651.795 57.529 1.00 56.49 8 6537 OW0 WAT W 195 15.790 48.084 23.036 1.0052.39 8 6538 OW0 WAT W 196 22.577 105.708 45.361 1.00 51.14 8 6539 OW0WAT W 197 7.453 103.921 23.508 1.00 50.15 8 6540 OW0 WAT W 198 37.89980.588 45.384 1.00 52.20 8 6541 OW0 WAT W 199 19.774 74.879 53.890 1.0055.07 8 6542 OW0 WAT W 200 50.055 68.873 30.956 1.00 30.00 8 6543 OW0WAT W 201 53.330 63.201 30.956 1.00 37.00 8 6544 OW0 WAT W 202 35.08689.130 21.284 1.00 49.00 8 6545 OW0 WAT W 203 2.339 51.858 35.796 1.0050.00 8 6546 OW0 WAT W 204 19.180 43.755 27.572 1.00 50.00 8 6547 OW0WAT W 205 51.693 55.504 46.921 1.00 51.00 8 6548 OW0 WAT W 206 31.81180.217 54.661 1.00 51.00 8 6549 OW0 WAT W 207 11.695 77.786 12.093 1.0051.00 8 6550 OW0 WAT W 208 29.940 46.996 53.693 1.00 52.00 8 6551 OW0WAT W 209 7.251 102.500 40.633 1.00 52.00 8 6552 OW0 WAT W 210 23.85891.561 17.414 1.00 52.00 8 6553 OW0 WAT W 211 6.783 49.832 40.633 1.0052.00 8 6554 OW0 WAT W 212 44.910 47.806 22.735 1.00 52.00 8 6555 OW0WAT W 213 36.255 46.591 10.158 1.00 52.00 8 6556 OW0 WAT W 214 27.60161.581 77.880 1.00 52.00 8 6557 OW0 WAT W 215 27.133 98.043 33.861 1.0053.00 8 6558 OW0 WAT W 216 18.479 55.504 45.470 1.00 53.00 8 6559 OW0WAT W 217 9.122 47.401 46.438 1.00 53.00 8 6560 OW0 WAT W 218 9.59066.037 16.447 1.00 53.00 8 6561 OW0 WAT W 219 13.333 91.966 46.438 1.0053.00 8

1. A method of preparing a maltogenic amylase variant having improvedanti-staling properties, which method comprises a) subjecting a DNAsequence encoding the maltogenic amylase to random mutagenesis, b)expressing the mutated DNA sequence obtained in step (a) in a host cell,and c) screening for host cells expressing a mutated maltogenic amylasewhich shows a higher thermostability, and d) preparing the mutatedmaltogenic amylase expressed by the host cells.
 2. The method of claim1, wherein the mutated DNA sequence is expressed by transforming asuitable host cell with the mutated DNA sequence and culturing the hostcell obtained in step (b) under suitable conditions for expressing themutated DNA sequence. 3-4. (canceled)
 5. A method of constructing avariant of a parent maltogenic alpha-amylase, which method comprises: a)identifying an amino acid residue which is within 15 Å (in particular 10Å) from an active site residue of the parent amylase in thethree-dimensional structure of said parent, and which is involved inelectrostatic or hydrophobic interactions with an active site residue;b) substituting said amino acid residue with another amino acid residuewhich changes the electrostatic and/or hydrophobic surroundings of anactive site residue, and which can be accommodated in the structure; c)optionally repeating steps a) and b) recursively; d) optionally, makingalterations each of which is an insertion, a deletion or a substitutionof an amino acid residue at one or more positions other than b), e)preparing the variant resulting from steps a)-d); f) testing the pHdependent activity of said variant; and g) optionally repeating stepsa)-f) recursively; and h) selecting a variant having an altered pHdependent activity as compared to the parent amylase. 6-9. (canceled)10. A polypeptide which: a) has maltogenic amylase activity; b) has atleast 70% identity to SEQ ID NO: 1, c) has optimum maltogenic amylaseactivity in the range pH 3.5-7.0 (preferably 4-5.5), and d) shows aresidual maltogenic amylase activity of at least 25% after incubationwith 1 mM Ca⁺⁺ at pH 4.3, 80° C. for 15 minutes. 11-34. (canceled)